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Outer membrane protein assembly factor BamA (Omp85)

 BAMA_ECOLI              Reviewed;         810 AA.
P0A940; P39170; P39181; P77465; Q548B8; Q8KR94; Q9R2E3;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
25-OCT-2017, entry version 118.
RecName: Full=Outer membrane protein assembly factor BamA {ECO:0000255|HAMAP-Rule:MF_01430};
AltName: Full=Omp85;
Flags: Precursor;
Name=bamA {ECO:0000255|HAMAP-Rule:MF_01430};
Synonyms=yaeT, yzzN, yzzY; OrderedLocusNames=b0177, JW0172;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11274153; DOI=10.1074/jbc.M100464200;
Dartigalongue C., Missiakas D., Raina S.;
"Characterization of the Escherichia coli sigma E regulon.";
J. Biol. Chem. 276:20866-20875(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
Allison H.E., Sergeant M.J., Cookson S.S., Yaxian Y., James C.E.,
Sharp R.J., Saunders J.R., McCarthy A.J.;
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
4.0 - 6.0 min (189,987 - 281,416bp) region.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
PROTEIN SEQUENCE OF 21-32 AND 351-362.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
POTRA DOMAIN.
PubMed=14559180; DOI=10.1016/j.tibs.2003.08.003;
Sanchez-Pulido L., Devos D., Genevrois S., Vicente M., Valencia A.;
"POTRA: a conserved domain in the FtsQ family and a class of beta-
barrel outer membrane proteins.";
Trends Biochem. Sci. 28:523-526(2003).
[9]
SUBUNIT, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=15851030; DOI=10.1016/j.cell.2005.02.015;
Wu T., Malinverni J., Ruiz N., Kim S., Silhavy T.J., Kahne D.;
"Identification of a multicomponent complex required for outer
membrane biogenesis in Escherichia coli.";
Cell 121:235-245(2005).
[10]
FUNCTION.
PubMed=15951436; DOI=10.1074/jbc.M504796200;
Doerrler W.T., Raetz C.R.H.;
"Loss of outer membrane proteins without inhibition of lipid export in
an Escherichia coli YaeT mutant.";
J. Biol. Chem. 280:27679-27687(2005).
[11]
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
PubMed=16079137; DOI=10.1074/jbc.M506479200;
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16102012; DOI=10.1111/j.1365-2958.2005.04775.x;
Werner J., Misra R.;
"YaeT (Omp85) affects the assembly of lipid-dependent and lipid-
independent outer membrane proteins of Escherichia coli.";
Mol. Microbiol. 57:1450-1459(2005).
[13]
FUNCTION, SUBUNIT, AND INTERACTION WITH BAMB AND BAMD.
STRAIN=K12;
PubMed=16824102; DOI=10.1111/j.1365-2958.2006.05211.x;
Malinverni J.C., Werner J., Kim S., Sklar J.G., Kahne D., Misra R.,
Silhavy T.J.;
"YfiO stabilizes the YaeT complex and is essential for outer membrane
protein assembly in Escherichia coli.";
Mol. Microbiol. 61:151-164(2006).
[14]
SUBUNIT.
STRAIN=K12;
PubMed=17404237; DOI=10.1073/pnas.0701579104;
Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D.,
Silhavy T.J.;
"Lipoprotein SmpA is a component of the YaeT complex that assembles
outer membrane proteins in Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 104:6400-6405(2007).
[15]
FUNCTION IN CDI, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC1061;
PubMed=18761695; DOI=10.1111/j.1365-2958.2008.06404.x;
Aoki S.K., Malinverni J.C., Jacoby K., Thomas B., Pamma R.,
Trinh B.N., Remers S., Webb J., Braaten B.A., Silhavy T.J., Low D.A.;
"Contact-dependent growth inhibition requires the essential outer
membrane protein BamA (YaeT) as the receptor and the inner membrane
transport protein AcrB.";
Mol. Microbiol. 70:323-340(2008).
[16]
FUNCTION, AND SUBUNIT.
PubMed=20378773; DOI=10.1126/science.1188919;
Hagan C.L., Kim S., Kahne D.;
"Reconstitution of outer membrane protein assembly from purified
components.";
Science 328:890-892(2010).
[17]
FUNCTION, AND SUBUNIT.
PubMed=21823654; DOI=10.1021/bi2010784;
Hagan C.L., Kahne D.;
"The reconstituted Escherichia coli Bam complex catalyzes multiple
rounds of beta-barrel assembly.";
Biochemistry 50:7444-7446(2011).
[18]
INTERACTION WITH BAMB AND BAMD.
PubMed=21586578; DOI=10.1074/jbc.M111.238931;
Albrecht R., Zeth K.;
"Structural basis of outer membrane protein biogenesis in bacteria.";
J. Biol. Chem. 286:27792-27803(2011).
[19]
FUNCTION IN CDI, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100;
PubMed=23469034; DOI=10.1371/journal.pone.0057609;
Webb J.S., Nikolakakis K.C., Willett J.L., Aoki S.K., Hayes C.S.,
Low D.A.;
"Delivery of CdiA nuclease toxins into target cells during contact-
dependent growth inhibition.";
PLoS ONE 8:E57609-E57609(2013).
[20]
FUNCTION IN CDI, STRAIN SPECIFICITY, SUBCELLULAR LOCATION, TOPOLOGY,
AND MUTAGENESIS OF 554-GLU--ASP-562; 556-PRO--SER-564;
675-PHE--SER-702; 677-HIS--ASP-685 AND 754-TYR-SER-755.
PubMed=23882017; DOI=10.1128/mBio.00480-13;
Ruhe Z.C., Wallace A.B., Low D.A., Hayes C.S.;
"Receptor polymorphism restricts contact-dependent growth inhibition
to members of the same species.";
MBio 4:E00480-E00480(2013).
[21] {ECO:0000244|PDB:2QCZ, ECO:0000244|PDB:2QDF}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 21-351, AND DOMAIN.
PubMed=17702946; DOI=10.1126/science.1143993;
Kim S., Malinverni J.C., Sliz P., Silhavy T.J., Harrison S.C.,
Kahne D.;
"Structure and function of an essential component of the outer
membrane protein assembly machine.";
Science 317:961-964(2007).
[22] {ECO:0000244|PDB:2V9H}
STRUCTURE BY NMR OF 21-184, AND DOMAIN.
PubMed=18430136; DOI=10.1111/j.1365-2958.2008.06225.x;
Knowles T.J., Jeeves M., Bobat S., Dancea F., McClelland D.,
Palmer T., Overduin M., Henderson I.R.;
"Fold and function of polypeptide transport-associated domains
responsible for delivering unfolded proteins to membranes.";
Mol. Microbiol. 68:1216-1227(2008).
[23] {ECO:0000244|PDB:3EFC}
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 21-410, AND DOMAIN.
PubMed=19081063; DOI=10.1016/j.str.2008.09.014;
Gatzeva-Topalova P.Z., Walton T.A., Sousa M.C.;
"Crystal structure of YaeT: conformational flexibility and substrate
recognition.";
Structure 16:1873-1881(2008).
[24] {ECO:0000244|PDB:3Q6B}
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 266-420, AND DOMAIN.
PubMed=21795783; DOI=10.1107/S1744309111014254;
Zhang H., Gao Z.Q., Hou H.F., Xu J.H., Li L.F., Su X.D., Dong Y.H.;
"High-resolution structure of a new crystal form of BamA POTRA4-5 from
Escherichia coli.";
Acta Crystallogr. F 67:734-738(2011).
[25] {ECO:0000244|PDB:4C4V}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 347-810 AND 344-810,
SUBCELLULAR LOCATION, DOMAIN, AND TOPOLOGY.
STRAIN=BL21 (DE3);
PubMed=24914988; DOI=10.1107/S1399004714007482;
Albrecht R., Schutz M., Oberhettinger P., Faulstich M., Bermejo I.,
Rudel T., Diederichs K., Zeth K.;
"Structure of BamA, an essential factor in outer membrane protein
biogenesis.";
Acta Crystallogr. D 70:1779-1789(2014).
[26] {ECO:0000244|PDB:4N75}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 427-810, SUBCELLULAR
LOCATION, DOMAIN, TOPOLOGY, AND MUTAGENESIS OF GLU-435; ASP-464;
ASP-500; ARG-547; ARG-661; 673-VAL--SER-702; ASP-740 AND GLU-800.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=24619089; DOI=10.1096/fj.13-248450;
Ni D., Wang Y., Yang X., Zhou H., Hou X., Cao B., Lu Z., Zhao X.,
Yang K., Huang Y.;
"Structural and functional analysis of the beta-barrel domain of BamA
from Escherichia coli.";
FASEB J. 28:2677-2685(2014).
[27] {ECO:0000244|PDB:5LJO}
STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 24-806 IN LATERAL
OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS
SPECTROMETRY, AND MUTAGENESIS OF ILE-430 AND LYS-808.
PubMed=27686148; DOI=10.1038/ncomms12865;
Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N.,
Brockwell D.J., Ashcroft A.E., Radford S.E., Ranson N.A.;
"Lateral opening in the intact beta-barrel assembly machinery captured
by cryo-EM.";
Nat. Commun. 7:12865-12865(2016).
[28] {ECO:0000244|PDB:5AYW}
X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 22-810 IN LATERAL CLOSED BAM
COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-181;
LYS-251; ASN-259 AND GLY-429.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=26900875; DOI=10.1038/nsmb.3181;
Han L., Zheng J., Wang Y., Yang X., Liu Y., Sun C., Cao B., Zhou H.,
Ni D., Lou J., Zhao Y., Huang Y.;
"Structure of the BAM complex and its implications for biogenesis of
outer-membrane proteins.";
Nat. Struct. Mol. Biol. 23:192-196(2016).
[29] {ECO:0000244|PDB:5D0O, ECO:0000244|PDB:5D0Q}
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX
AND LATERAL OPEN BAMACDE SUBCOMPLEX, REACTION MECHANISM, SUBUNIT,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 351-LYS--LYS-353; LYS-351;
ARG-366; GLU-373; GLY-393; 415-VAL--LYS-419; 415-VAL--LYS-417;
417-LYS--LYS-419; GLU-435; GLY-584 AND SER-658.
PubMed=26901871; DOI=10.1038/nature17199;
Gu Y., Li H., Dong H., Zeng Y., Zhang Z., Paterson N.G.,
Stansfeld P.J., Wang Z., Zhang Y., Wang W., Dong C.;
"Structural basis of outer membrane protein insertion by the BAM
complex.";
Nature 531:64-69(2016).
[30] {ECO:0000244|PDB:5EKQ}
X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 21-810 OF LATERAL OPEN
BAMACDE SUBCOMPLEX, AND SUBUNIT.
PubMed=26744406; DOI=10.1126/science.aad3460;
Bakelar J., Buchanan S.K., Noinaj N.;
"The structure of the beta-barrel assembly machinery complex.";
Science 351:180-186(2016).
-!- FUNCTION: Part of the outer membrane protein assembly complex
(Bam), which is involved in assembly and insertion of beta-barrel
proteins into the outer membrane. Constitutes, with BamD, the core
component of the assembly machinery. Efficient substrate folding
and insertion into the outer membrane requires all 5 subunits
(PubMed:20378773, PubMed:21823654, PubMed:27686148). A lateral
gate may open between the first and last strands of the BamA beta-
barrel that allows substrate to insert into the outer membrane;
comparison of the structures of complete and nearly complete Bam
complexes show there is considerable movement of all 5 proteins
(PubMed:27686148, PubMed:26900875, PubMed:26901871,
PubMed:26744406). {ECO:0000269|PubMed:15951436,
ECO:0000269|PubMed:16102012, ECO:0000269|PubMed:16824102,
ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21823654,
ECO:0000269|PubMed:26744406, ECO:0000269|PubMed:26900875,
ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:27686148}.
-!- FUNCTION: Acts as a receptor for CdiA-EC93, the contact-dependent
growth inhibition (CDI) effector of E.coli strain EC93; antibodies
against extracellular epitopes decrease CDI. Its role in CDI is
independent of the other Bam complex components (PubMed:18761695).
Also acts as a receptor for CDI with CdiA from E.coli strain 536 /
UPEC, which does not have the same mode of toxicity as CdiA from
strain EC93 (PubMed:23469034, PubMed:23882017). Susceptibility to
CdiA-EC93 is dependent on E.coli BamA; replacing BamA with the
gene from S.typhimurium LT2, E.cloacae ATCC 13047 or D.dadantii
3937 renders cells resistant to CdiA-EC93. Cells with BamA from
another bacteria no longer form CdiA-EC93-induced aggregates with
EC93 cells. A chimera in which E.cloacae extracellular loops 6 and
7 are replaced with loops 6 and 7 from E.coli is susceptible to
CdiA-EC93 and to CdiA-CT from strain 536 / UPEC (PubMed:23882017).
{ECO:0000269|PubMed:18761695, ECO:0000269|PubMed:23469034,
ECO:0000269|PubMed:23882017}.
-!- SUBUNIT: Part of the Bam complex, which is composed of the outer
membrane protein BamA, and four lipoproteins BamB, BamC, BamD and
BamE. BamA interacts directly with BamB and the BamCDE subcomplex.
The Bam complex has the shape of a hat, with the BamA beta-barrel
crown in the outer membrane and the periplasmic brim formed by the
BamA POTRA domains and the 4 lipoproteins (PubMed:27686148,
PubMed:26900875, PubMed:26901871, PubMed:26744406).
{ECO:0000269|PubMed:15851030, ECO:0000269|PubMed:16079137,
ECO:0000269|PubMed:16824102, ECO:0000269|PubMed:17404237,
ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21586578,
ECO:0000269|PubMed:21823654, ECO:0000269|PubMed:26900875,
ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:27686148}.
-!- INTERACTION:
P77774:bamB; NbExp=23; IntAct=EBI-907371, EBI-907297;
P0AC02:bamD; NbExp=26; IntAct=EBI-907371, EBI-1128087;
P69411:rcsF; NbExp=3; IntAct=EBI-907371, EBI-1114706;
-!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
Rule:MF_01430, ECO:0000269|PubMed:16079137,
ECO:0000269|PubMed:23882017, ECO:0000269|PubMed:24619089,
ECO:0000269|PubMed:24914988, ECO:0000269|PubMed:26901871,
ECO:0000269|PubMed:9298646}.
-!- DOMAIN: Contains 5 N-terminal periplasmic polypeptide transport-
associated (POTRA) domains which interact with other subunits of
the complex, may recruit substrates from the periplasm into the
outer membrane and also act as a chaperone (PubMed:17702946,
PubMed:18430136, PubMed:19081063, PubMed:21795783,
PubMed:14559180). The C-terminal region forms a discontinuous 16-
stranded beta-barrel transmembrane region. The central pore is
ellipsoid, and probably closed by extracellular loop 6, perhaps
with the aid of other loops (PubMed:24914988, PubMed:24619089).
{ECO:0000269|PubMed:17702946, ECO:0000269|PubMed:18430136,
ECO:0000269|PubMed:19081063, ECO:0000269|PubMed:21795783,
ECO:0000269|PubMed:24619089, ECO:0000269|PubMed:24914988,
ECO:0000305|PubMed:14559180}.
-!- MASS SPECTROMETRY: Mass=88426; Method=Electrospray; Range=21-810;
Evidence={ECO:0000269|PubMed:27686148};
-!- DISRUPTION PHENOTYPE: Deletion is lethal. Depletion results in the
accumulation of incorrectly assembled outer membrane proteins,
including TolC, OmpF, OmpC and OmpA (PubMed:15851030,
PubMed:16102012). Decreased expression leads to decreased
susceptibility to contact-dependent growth inhibition (CDI), and
decreased expression of outer membrane proteins (including in this
study LamB) as well as up-regulation of periplasmic protease DegP
(PubMed:18761695, PubMed:23469034). {ECO:0000269|PubMed:15851030,
ECO:0000269|PubMed:16102012, ECO:0000269|PubMed:18761695,
ECO:0000269|PubMed:23469034}.
-!- SIMILARITY: Belongs to the BamA family. {ECO:0000255|HAMAP-
Rule:MF_01430}.
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EMBL; AF407013; AAL01379.1; -; Genomic_DNA.
EMBL; AY035865; AAK64508.1; -; Genomic_DNA.
EMBL; U70214; AAB08606.1; -; Genomic_DNA.
EMBL; U00096; AAC73288.1; -; Genomic_DNA.
EMBL; AP009048; BAA77852.2; -; Genomic_DNA.
PIR; A64742; A64742.
RefSeq; NP_414719.1; NC_000913.3.
RefSeq; WP_001240896.1; NZ_LN832404.1.
PDB; 2QCZ; X-ray; 2.70 A; A/B=21-351.
PDB; 2QDF; X-ray; 2.20 A; A=21-351.
PDB; 2V9H; NMR; -; A=21-184.
PDB; 3EFC; X-ray; 3.30 A; A=21-410.
PDB; 3OG5; X-ray; 2.69 A; A/B=264-424.
PDB; 3Q6B; X-ray; 1.50 A; A=266-420.
PDB; 4C4V; X-ray; 3.00 A; A=347-810, B=344-810.
PDB; 4N75; X-ray; 2.60 A; A/B=427-810.
PDB; 4PK1; X-ray; 3.10 A; A=175-424.
PDB; 4XGA; X-ray; 2.15 A; B=175-420.
PDB; 5AYW; X-ray; 3.56 A; A=22-810.
PDB; 5D0O; X-ray; 2.90 A; A=1-810.
PDB; 5D0Q; X-ray; 3.50 A; A/F=1-810.
PDB; 5EKQ; X-ray; 3.39 A; A=21-810.
PDB; 5LJO; EM; 4.90 A; A=24-806.
PDBsum; 2QCZ; -.
PDBsum; 2QDF; -.
PDBsum; 2V9H; -.
PDBsum; 3EFC; -.
PDBsum; 3OG5; -.
PDBsum; 3Q6B; -.
PDBsum; 4C4V; -.
PDBsum; 4N75; -.
PDBsum; 4PK1; -.
PDBsum; 4XGA; -.
PDBsum; 5AYW; -.
PDBsum; 5D0O; -.
PDBsum; 5D0Q; -.
PDBsum; 5EKQ; -.
PDBsum; 5LJO; -.
ProteinModelPortal; P0A940; -.
SMR; P0A940; -.
BioGrid; 4259504; 695.
DIP; DIP-36019N; -.
IntAct; P0A940; 14.
STRING; 316385.ECDH10B_0157; -.
SWISS-2DPAGE; P0A940; -.
PaxDb; P0A940; -.
PRIDE; P0A940; -.
EnsemblBacteria; AAC73288; AAC73288; b0177.
EnsemblBacteria; BAA77852; BAA77852; BAA77852.
GeneID; 944870; -.
KEGG; ecj:JW0172; -.
KEGG; eco:b0177; -.
PATRIC; fig|1411691.4.peg.2102; -.
EchoBASE; EB2541; -.
EcoGene; EG12676; bamA.
eggNOG; ENOG4105E1Z; Bacteria.
eggNOG; COG4775; LUCA.
InParanoid; P0A940; -.
KO; K07277; -.
PhylomeDB; P0A940; -.
BioCyc; EcoCyc:G6093-MONOMER; -.
EvolutionaryTrace; P0A940; -.
PRO; PR:P0A940; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:1990063; C:Bam protein complex; IDA:EcoCyc.
GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IDA:EcoCyc.
GO; GO:0051205; P:protein insertion into membrane; IDA:EcoCyc.
HAMAP; MF_01430; OM_assembly_BamA; 1.
InterPro; IPR000184; Bac_surfAg_D15.
InterPro; IPR010827; BamA/TamA_POTRA.
InterPro; IPR023707; OM_assembly_BamA.
InterPro; IPR034746; POTRA.
Pfam; PF01103; Bac_surface_Ag; 1.
Pfam; PF07244; POTRA; 4.
PIRSF; PIRSF006076; OM_assembly_OMP85; 1.
TIGRFAMs; TIGR03303; OM_YaeT; 1.
PROSITE; PS51779; POTRA; 5.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell outer membrane; Complete proteome;
Direct protein sequencing; Membrane; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane beta strand.
SIGNAL 1 20 {ECO:0000255|HAMAP-Rule:MF_01430,
ECO:0000269|PubMed:9298646}.
CHAIN 21 810 Outer membrane protein assembly factor
BamA.
/FTId=PRO_0000033470.
TOPO_DOM 21 424 Periplasmic. {ECO:0000305}.
TRANSMEM 425 433 Beta stranded; Name=Strand 1.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 434 435 Extracellular; loop 1. {ECO:0000305}.
TRANSMEM 436 446 Beta stranded; Name=Strand 2.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 447 454 Periplasmic. {ECO:0000305}.
TRANSMEM 455 462 Beta stranded; Name=Strand 3.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 463 465 Extracellular; loop 2. {ECO:0000305}.
TRANSMEM 466 475 Beta stranded; Name=Strand 4.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 476 483 Periplasmic. {ECO:0000305}.
TRANSMEM 484 495 Beta stranded; Name=Strand 5.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 496 504 Extracellular; loop 3. {ECO:0000305}.
TRANSMEM 505 506 Beta stranded; Name=Strand 6.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 507 522 Periplasmic. {ECO:0000305}.
TRANSMEM 523 535 Beta stranded; Name=Strand 7.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 536 563 Extracellular; loop 4.
{ECO:0000269|PubMed:23882017,
ECO:0000269|PubMed:24914988}.
TRANSMEM 564 577 Beta stranded; Name=Strand 8.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 578 590 Periplasmic. {ECO:0000305}.
TRANSMEM 591 600 Beta stranded; Name=Strand 9.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 601 608 Extracellular; loop 5. {ECO:0000305}.
TRANSMEM 609 619 Beta stranded; Name=Strand 10.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 620 628 Periplasmic. {ECO:0000305}.
TRANSMEM 629 639 Beta stranded; Name=Strand 11.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 640 708 Extracellular; loop 6.
{ECO:0000269|PubMed:23882017,
ECO:0000269|PubMed:24914988}.
TRANSMEM 709 718 Beta stranded; Name=Strand 12.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 719 732 Periplasmic. {ECO:0000305}.
TRANSMEM 733 745 Beta stranded; Name=Strand 13.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 746 767 Extracellular; loop 7. {ECO:0000305}.
TRANSMEM 768 777 Beta stranded; Name=Strand 14.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 778 778 Periplasmic. {ECO:0000305}.
TRANSMEM 779 789 Beta stranded; Name=Strand 15.
{ECO:0000269|PubMed:24914988}.
TOPO_DOM 790 803 Extracellular; loop 8. {ECO:0000305}.
TRANSMEM 804 808 Beta stranded; Name=Strand 16.
{ECO:0000269|PubMed:24914988}.
DOMAIN 24 91 POTRA 1. {ECO:0000255|PROSITE-
ProRule:PRU01115,
ECO:0000305|PubMed:14559180}.
DOMAIN 92 172 POTRA 2. {ECO:0000255|PROSITE-
ProRule:PRU01115,
ECO:0000305|PubMed:14559180}.
DOMAIN 175 263 POTRA 3. {ECO:0000255|PROSITE-
ProRule:PRU01115,
ECO:0000305|PubMed:14559180}.
DOMAIN 266 344 POTRA 4. {ECO:0000255|PROSITE-
ProRule:PRU01115,
ECO:0000305|PubMed:14559180}.
DOMAIN 347 421 POTRA 5. {ECO:0000255|PROSITE-
ProRule:PRU01115,
ECO:0000305|PubMed:14559180}.
MUTAGEN 181 181 N->A: Lethal, protein does not
accumulate.
{ECO:0000269|PubMed:26900875}.
MUTAGEN 251 251 K->A: Lethal, protein does not
accumulate.
{ECO:0000269|PubMed:26900875}.
MUTAGEN 259 259 N->A: Lethal, protein does not
accumulate.
{ECO:0000269|PubMed:26900875}.
MUTAGEN 351 353 KIR->PIP: Lethal, wild-type protein
levels. {ECO:0000269|PubMed:26901871}.
MUTAGEN 351 351 K->P: Reduces cell growth, wild-type
protein levels.
{ECO:0000269|PubMed:26901871}.
MUTAGEN 366 366 R->E: Severely impairs cell growth, wild-
type protein levels.
{ECO:0000269|PubMed:26901871}.
MUTAGEN 373 373 E->K: Lethal, wild-type protein levels.
{ECO:0000269|PubMed:26900875,
ECO:0000269|PubMed:26901871}.
MUTAGEN 393 393 G->C: No effect. Lethal; when associated
with C-584, probably locks protein in a
single conformation that prevents
movement, growth restored by strong
reducing agent.
{ECO:0000269|PubMed:26901871}.
MUTAGEN 415 419 VYKVK->PYKVP: Lethal, wild-type protein
levels. {ECO:0000269|PubMed:26901871}.
MUTAGEN 415 417 VYK->PYP: Lethal, wild-type protein
levels. {ECO:0000269|PubMed:26901871}.
MUTAGEN 417 419 KVK->PVP: Lethal, wild-type protein
levels. {ECO:0000269|PubMed:26901871}.
MUTAGEN 429 429 G->P: Lethal, wild-type protein levels.
{ECO:0000269|PubMed:26900875}.
MUTAGEN 430 430 I->C: Reduced folding of OmpT; when
associated with C-808, traps protein in
lateral closed conformation, growth
restored by reducing agent.
{ECO:0000269|PubMed:27686148}.
MUTAGEN 435 435 E->C: No effect. Lethal; when associated
with C-658 or C-665, probably locks
protein in a single conformation that
prevents movement, growth restored by
strong reducing agent.
{ECO:0000269|PubMed:26901871}.
MUTAGEN 435 435 E->L: Very minor growth defect. Lethal;
when associated with L-800.
{ECO:0000269|PubMed:24619089}.
MUTAGEN 464 464 D->L: Very minor growth defect.
{ECO:0000269|PubMed:24619089}.
MUTAGEN 500 500 D->L: Very minor growth defect.
{ECO:0000269|PubMed:24619089}.
MUTAGEN 547 547 R->A: Lethal.
{ECO:0000269|PubMed:24619089}.
MUTAGEN 554 562 EHPSTSDQD->VDYPYDVPDYA: Loop 4 to HA
epitope; still susceptible to CdiA-EC93.
{ECO:0000269|PubMed:23882017}.
MUTAGEN 556 563 PSTSDQDN->G: Delta loop 4; slight
increase in resistance to CdiA-EC93,
forms aggregates with CdiA-EC93 cells.
{ECO:0000269|PubMed:23882017}.
MUTAGEN 584 584 G->C: No effect. Lethal; when associated
with C-393, probably locks protein in a
single conformation that prevents
movement, growth restored by strong
reducing agent.
{ECO:0000269|PubMed:26901871}.
MUTAGEN 658 658 S->C: No effect. Lethal; when associated
with C-435, probably locks protein in a
single conformation that prevents
movement, growth restored by strong
reducing agent.
{ECO:0000269|PubMed:26901871}.
MUTAGEN 661 661 R->A: Slow growth on solid and liquid
media, less protein accumulates which is
more proteinase sensitive.
{ECO:0000269|PubMed:24619089}.
MUTAGEN 665 665 S->C: No effect. Lethal; when associated
with C-435, probably locks protein in a
single conformation that prevents
movement, growth restored by strong
reducing agent.
{ECO:0000269|PubMed:26901871}.
MUTAGEN 673 702 Missing: Lethal.
{ECO:0000269|PubMed:24619089}.
MUTAGEN 675 701 FPHQASNYDPDYDYECATQDGAKDLCK->G: Delta
loop 6; fully resistant to CdiA-EC93,
does not form aggregates with CdiA-EC93
cells. {ECO:0000269|PubMed:23882017}.
MUTAGEN 677 685 HQASNYDPD->VDYPYDVPDYA: Loop 6 to HA
epitope; still susceptible to CdiA-EC93.
{ECO:0000269|PubMed:23882017}.
MUTAGEN 740 740 D->A: Slow growth on solid and liquid
media, less protein accumulates which is
more proteinase sensitive.
{ECO:0000269|PubMed:24619089}.
MUTAGEN 754 755 YS->VDYPYDVPDYA: Loop 7 to HA epitope;
fully resistant to CdiA-EC93, does not
form aggregates with CdiA-EC93 cells.
{ECO:0000269|PubMed:23882017}.
MUTAGEN 800 800 E->L: Very minor growth defect. Lethal;
when associated with L-435.
{ECO:0000269|PubMed:24619089}.
MUTAGEN 808 808 K->C: Reduced folding of OmpT; when
associated with C-430, traps protein in
lateral closed conformation, growth
restored by reducing agent.
{ECO:0000269|PubMed:27686148}.
CONFLICT 115 115 E -> Q (in Ref. 2; AAK64508).
{ECO:0000305}.
CONFLICT 228 228 S -> I (in Ref. 2; AAK64508).
{ECO:0000305}.
CONFLICT 361 361 K -> R (in Ref. 2; AAK64508).
{ECO:0000305}.
CONFLICT 632 632 R -> C (in Ref. 2; AAK64508).
{ECO:0000305}.
CONFLICT 712 712 A -> T (in Ref. 2; AAK64508).
{ECO:0000305}.
STRAND 28 33 {ECO:0000244|PDB:2QDF}.
STRAND 35 37 {ECO:0000244|PDB:2QDF}.
HELIX 39 44 {ECO:0000244|PDB:2QDF}.
HELIX 56 67 {ECO:0000244|PDB:2QDF}.
STRAND 72 80 {ECO:0000244|PDB:2QDF}.
STRAND 83 90 {ECO:0000244|PDB:2QDF}.
STRAND 93 101 {ECO:0000244|PDB:2QDF}.
STRAND 103 105 {ECO:0000244|PDB:2QCZ}.
HELIX 107 115 {ECO:0000244|PDB:2QDF}.
TURN 116 118 {ECO:0000244|PDB:2QDF}.
STRAND 121 123 {ECO:0000244|PDB:3EFC}.
HELIX 127 129 {ECO:0000244|PDB:3EFC}.
HELIX 130 140 {ECO:0000244|PDB:2QDF}.
HELIX 141 144 {ECO:0000244|PDB:2QDF}.
STRAND 146 148 {ECO:0000244|PDB:2QDF}.
STRAND 150 158 {ECO:0000244|PDB:2QDF}.
TURN 159 161 {ECO:0000244|PDB:2QDF}.
STRAND 162 170 {ECO:0000244|PDB:2QDF}.
STRAND 176 184 {ECO:0000244|PDB:4XGA}.
STRAND 186 188 {ECO:0000244|PDB:2QCZ}.
HELIX 190 194 {ECO:0000244|PDB:4XGA}.
HELIX 195 197 {ECO:0000244|PDB:2QDF}.
TURN 210 212 {ECO:0000244|PDB:3EFC}.
HELIX 216 231 {ECO:0000244|PDB:4XGA}.
TURN 232 234 {ECO:0000244|PDB:4XGA}.
STRAND 239 247 {ECO:0000244|PDB:4XGA}.
STRAND 251 261 {ECO:0000244|PDB:4XGA}.
STRAND 267 276 {ECO:0000244|PDB:3Q6B}.
TURN 278 280 {ECO:0000244|PDB:5D0O}.
HELIX 281 287 {ECO:0000244|PDB:3Q6B}.
HELIX 298 313 {ECO:0000244|PDB:3Q6B}.
TURN 314 316 {ECO:0000244|PDB:3Q6B}.
STRAND 317 319 {ECO:0000244|PDB:4XGA}.
STRAND 321 329 {ECO:0000244|PDB:3Q6B}.
TURN 330 333 {ECO:0000244|PDB:3Q6B}.
STRAND 334 342 {ECO:0000244|PDB:3Q6B}.
STRAND 348 356 {ECO:0000244|PDB:3Q6B}.
STRAND 358 360 {ECO:0000244|PDB:3Q6B}.
HELIX 362 366 {ECO:0000244|PDB:3Q6B}.
STRAND 373 376 {ECO:0000244|PDB:4C4V}.
HELIX 379 392 {ECO:0000244|PDB:3Q6B}.
STRAND 396 405 {ECO:0000244|PDB:3Q6B}.
STRAND 408 419 {ECO:0000244|PDB:3Q6B}.
STRAND 427 433 {ECO:0000244|PDB:4N75}.
TURN 434 436 {ECO:0000244|PDB:4N75}.
STRAND 437 453 {ECO:0000244|PDB:4N75}.
STRAND 455 462 {ECO:0000244|PDB:4N75}.
STRAND 464 475 {ECO:0000244|PDB:4N75}.
TURN 479 482 {ECO:0000244|PDB:4C4V}.
STRAND 484 495 {ECO:0000244|PDB:4N75}.
HELIX 496 499 {ECO:0000244|PDB:4N75}.
STRAND 501 503 {ECO:0000244|PDB:4N75}.
STRAND 505 520 {ECO:0000244|PDB:4N75}.
STRAND 523 537 {ECO:0000244|PDB:4N75}.
HELIX 543 551 {ECO:0000244|PDB:4N75}.
STRAND 558 561 {ECO:0000244|PDB:5EKQ}.
STRAND 564 579 {ECO:0000244|PDB:4N75}.
STRAND 584 586 {ECO:0000244|PDB:4N75}.
STRAND 589 600 {ECO:0000244|PDB:4N75}.
STRAND 604 606 {ECO:0000244|PDB:5D0O}.
STRAND 608 620 {ECO:0000244|PDB:4N75}.
STRAND 622 625 {ECO:0000244|PDB:4C4V}.
STRAND 627 643 {ECO:0000244|PDB:4N75}.
HELIX 648 650 {ECO:0000244|PDB:4N75}.
STRAND 656 660 {ECO:0000244|PDB:5EKQ}.
STRAND 671 674 {ECO:0000244|PDB:5D0O}.
STRAND 685 687 {ECO:0000244|PDB:4N75}.
STRAND 689 691 {ECO:0000244|PDB:5D0O}.
HELIX 692 694 {ECO:0000244|PDB:5D0O}.
STRAND 700 705 {ECO:0000244|PDB:5D0O}.
STRAND 708 720 {ECO:0000244|PDB:4N75}.
STRAND 723 725 {ECO:0000244|PDB:5D0O}.
TURN 727 731 {ECO:0000244|PDB:5D0O}.
STRAND 733 745 {ECO:0000244|PDB:4N75}.
TURN 751 756 {ECO:0000244|PDB:4N75}.
STRAND 767 778 {ECO:0000244|PDB:4N75}.
STRAND 781 792 {ECO:0000244|PDB:4N75}.
STRAND 802 809 {ECO:0000244|PDB:4N75}.
SEQUENCE 810 AA; 90553 MW; DDCE4C6D341664EB CRC64;
MAMKKLLIAS LLFSSATVYG AEGFVVKDIH FEGLQRVAVG AALLSMPVRT GDTVNDEDIS
NTIRALFATG NFEDVRVLRD GDTLLVQVKE RPTIASITFS GNKSVKDDML KQNLEASGVR
VGESLDRTTI ADIEKGLEDF YYSVGKYSAS VKAVVTPLPR NRVDLKLVFQ EGVSAEIQQI
NIVGNHAFTT DELISHFQLR DEVPWWNVVG DRKYQKQKLA GDLETLRSYY LDRGYARFNI
DSTQVSLTPD KKGIYVTVNI TEGDQYKLSG VEVSGNLAGH SAEIEQLTKI EPGELYNGTK
VTKMEDDIKK LLGRYGYAYP RVQSMPEIND ADKTVKLRVN VDAGNRFYVR KIRFEGNDTS
KDAVLRREMR QMEGAWLGSD LVDQGKERLN RLGFFETVDT DTQRVPGSPD QVDVVYKVKE
RNTGSFNFGI GYGTESGVSF QAGVQQDNWL GTGYAVGING TKNDYQTYAE LSVTNPYFTV
DGVSLGGRLF YNDFQADDAD LSDYTNKSYG TDVTLGFPIN EYNSLRAGLG YVHNSLSNMQ
PQVAMWRYLY SMGEHPSTSD QDNSFKTDDF TFNYGWTYNK LDRGYFPTDG SRVNLTGKVT
IPGSDNEYYK VTLDTATYVP IDDDHKWVVL GRTRWGYGDG LGGKEMPFYE NFYAGGSSTV
RGFQSNTIGP KAVYFPHQAS NYDPDYDYEC ATQDGAKDLC KSDDAVGGNA MAVASLEFIT
PTPFISDKYA NSVRTSFFWD MGTVWDTNWD SSQYSGYPDY SDPSNIRMSA GIALQWMSPL
GPLVFSYAQP FKKYDGDKAE QFQFNIGKTW


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