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Outer-membrane lipoprotein carrier protein (P20)

 LOLA_ECOLI              Reviewed;         203 AA.
P61316; P39178; Q8X5H8;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 1.
10-OCT-2018, entry version 133.
RecName: Full=Outer-membrane lipoprotein carrier protein;
AltName: Full=P20;
Flags: Precursor;
Name=lolA; Synonyms=lplA, yzzV; OrderedLocusNames=b0891, JW0874;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 22-39;
45-60; 64-81; 104-115 AND 188-203.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=7628437;
Matsuyama S., Tajima T., Tokuda H.;
"A novel periplasmic carrier protein involved in the sorting and
transport of Escherichia coli lipoproteins destined for the outer
membrane.";
EMBO J. 14:3365-3372(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
[5]
PROTEIN SEQUENCE OF 22-33.
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).
[6]
FUNCTION IN THE REGULATION OF THE RCS SYSTEM.
PubMed=11758943; DOI=10.1271/bbb.65.2364;
Chen M.H., Takeda S., Yamada H., Ishii Y., Yamashino T., Mizuno T.;
"Characterization of the RcsC->YojN->RcsB phosphorelay signaling
pathway involved in capsular synthesis in Escherichia coli.";
Biosci. Biotechnol. Biochem. 65:2364-2367(2001).
[7]
CHARACTERIZATION OF SORTING SIGNALS.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11592971; DOI=10.1074/jbc.M109307200;
Terada M., Kuroda T., Matsuyama S., Tokuda H.;
"Lipoprotein sorting signals evaluated as the LolA-dependent release
of lipoproteins from the cytoplasmic membrane of Escherichia coli.";
J. Biol. Chem. 276:47690-47694(2001).
[8]
CHARACTERIZATION OF SORTING SIGNALS.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=12032293; DOI=10.1073/pnas.112085599;
Masuda K., Matsuyama S., Tokuda H.;
"Elucidation of the function of lipoprotein-sorting signals that
determine membrane localization.";
Proc. Natl. Acad. Sci. U.S.A. 99:7390-7395(2002).
[9]
REQUIREMENT OF AMINOACYLATION FOR RELEASE OF LIPOPROTEINS.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=12198129; DOI=10.1074/jbc.M206816200;
Fukuda A., Matsuyama S., Hara T., Nakayama J., Nagasawa H., Tokuda H.;
"Aminoacylation of the N-terminal cysteine is essential for Lol-
dependent release of lipoproteins from membranes but does not depend
on lipoprotein sorting signals.";
J. Biol. Chem. 277:43512-43518(2002).
[10]
MUTAGENESIS OF ARG-64.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11587539; DOI=10.1006/bbrc.2001.5705;
Miyamoto A., Matsuyama S., Tokuda H.;
"Mutant of LolA, a lipoprotein-specific molecular chaperone of
Escherichia coli, defective in the transfer of lipoproteins to LolB.";
Biochem. Biophys. Res. Commun. 287:1125-1128(2001).
[11]
MUTAGENESIS OF PHE-68.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=12297303; DOI=10.1016/S0014-5793(02)03305-7;
Miyamoto A., Matsuyama S., Tokuda H.;
"Dominant negative mutant of a lipoprotein-specific molecular
chaperone, LolA, tightly associates with LolCDE.";
FEBS Lett. 528:193-196(2002).
[12]
CRYSTALLIZATION.
PubMed=12876347; DOI=10.1107/S090744490301254X;
Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., Miki K.;
"A practical phasing procedure using the MAD method without the aid of
XAFS measurements: successful solution in the structure determination
of the outer-membrane lipoprotein carrier LolA.";
Acta Crystallogr. D 59:1440-1446(2003).
[13]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
PubMed=12839983; DOI=10.1093/emboj/cdg324;
Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., Miki K.;
"Crystal structures of bacterial lipoprotein localization factors,
LolA and LolB.";
EMBO J. 22:3199-3209(2003).
-!- FUNCTION: Participates in the translocation of lipoproteins from
the inner membrane to the outer membrane. Only forms a complex
with a lipoprotein if the residue after the N-terminal Cys is not
an aspartate (The Asp acts as a targeting signal to indicate that
the lipoprotein should stay in the inner membrane); the inner
membrane retention signal functions at the release step.
{ECO:0000269|PubMed:11758943}.
-!- FUNCTION: May act as a regulator of the RCS-phosphorelay signal
transduction pathway. {ECO:0000269|PubMed:11758943}.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
P61320:lolB; NbExp=2; IntAct=EBI-553532, EBI-1122794;
P0ADC3:lolC; NbExp=2; IntAct=EBI-553532, EBI-15765497;
P0A912:pal; NbExp=2; IntAct=EBI-553532, EBI-1124760;
-!- SUBCELLULAR LOCATION: Periplasm.
-!- SIMILARITY: Belongs to the LolA family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA08390.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA35616.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D49398; BAA08390.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC73977.2; -; Genomic_DNA.
EMBL; AP009048; BAA35616.1; ALT_INIT; Genomic_DNA.
PIR; S57828; S57828.
RefSeq; NP_415411.2; NC_000913.3.
RefSeq; WP_001295343.1; NZ_LN832404.1.
PDB; 1IWL; X-ray; 1.65 A; A=22-203.
PDB; 1UA8; X-ray; 1.90 A; A=22-203.
PDB; 2ZPC; X-ray; 2.35 A; A=22-203.
PDB; 2ZPD; X-ray; 1.85 A; A=22-203.
PDB; 3KSN; X-ray; 1.65 A; A=22-203.
PDB; 6F3Z; X-ray; 2.00 A; B/D=22-203.
PDB; 6FHM; X-ray; 2.39 A; A/B=22-203.
PDBsum; 1IWL; -.
PDBsum; 1UA8; -.
PDBsum; 2ZPC; -.
PDBsum; 2ZPD; -.
PDBsum; 3KSN; -.
PDBsum; 6F3Z; -.
PDBsum; 6FHM; -.
ProteinModelPortal; P61316; -.
SMR; P61316; -.
BioGrid; 4260649; 338.
DIP; DIP-35675N; -.
IntAct; P61316; 13.
MINT; P61316; -.
STRING; 316385.ECDH10B_0961; -.
ChEMBL; CHEMBL3309024; -.
TCDB; 1.B.46.1.1; the outer membrane lolab lipoprotein insertion apparatus (lolab) family.
SWISS-2DPAGE; P61316; -.
EPD; P61316; -.
PaxDb; P61316; -.
PRIDE; P61316; -.
EnsemblBacteria; AAC73977; AAC73977; b0891.
EnsemblBacteria; BAA35616; BAA35616; BAA35616.
GeneID; 948989; -.
KEGG; ecj:JW0874; -.
KEGG; eco:b0891; -.
PATRIC; fig|1411691.4.peg.1386; -.
EchoBASE; EB2548; -.
EcoGene; EG12684; lolA.
eggNOG; ENOG4107Y7W; Bacteria.
eggNOG; COG2834; LUCA.
HOGENOM; HOG000257501; -.
InParanoid; P61316; -.
KO; K03634; -.
OMA; YDPFVEQ; -.
PhylomeDB; P61316; -.
BioCyc; EcoCyc:G6465-MONOMER; -.
EvolutionaryTrace; P61316; -.
PRO; PR:P61316; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0042954; F:lipoprotein transporter activity; IDA:EcoCyc.
GO; GO:0072323; P:chaperone-mediated protein transport across periplasmic space; IDA:CACAO.
GO; GO:0044874; P:lipoprotein localization to outer membrane; IDA:CACAO.
GO; GO:0042953; P:lipoprotein transport; IDA:EcoCyc.
CDD; cd16325; LolA; 1.
HAMAP; MF_00240; LolA; 1.
InterPro; IPR029046; LolA/LolB/LppX.
InterPro; IPR004564; OM_lipoprot_carrier_LolA-like.
InterPro; IPR018323; OM_lipoprot_carrier_LolA_Pbac.
PANTHER; PTHR35869; PTHR35869; 1.
Pfam; PF03548; LolA; 1.
SUPFAM; SSF89392; SSF89392; 1.
TIGRFAMs; TIGR00547; lolA; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Direct protein sequencing;
Periplasm; Protein transport; Reference proteome; Signal; Transport.
SIGNAL 1 21 {ECO:0000269|PubMed:7628437,
ECO:0000269|PubMed:9298646}.
CHAIN 22 203 Outer-membrane lipoprotein carrier
protein.
/FTId=PRO_0000018256.
MUTAGEN 64 64 R->L: Loss of ability to transfer
lipoproteins to LolB.
{ECO:0000269|PubMed:11587539}.
MUTAGEN 68 68 F->E: Loss of ability to bind
lipoproteins.
{ECO:0000269|PubMed:12297303}.
HELIX 23 30 {ECO:0000244|PDB:1IWL}.
STRAND 35 46 {ECO:0000244|PDB:1IWL}.
STRAND 48 51 {ECO:0000244|PDB:2ZPC}.
STRAND 54 63 {ECO:0000244|PDB:1IWL}.
TURN 64 66 {ECO:0000244|PDB:1IWL}.
STRAND 67 72 {ECO:0000244|PDB:1IWL}.
STRAND 74 76 {ECO:0000244|PDB:1IWL}.
STRAND 78 91 {ECO:0000244|PDB:1IWL}.
HELIX 92 94 {ECO:0000244|PDB:1IWL}.
STRAND 96 101 {ECO:0000244|PDB:1IWL}.
HELIX 102 104 {ECO:0000244|PDB:1IWL}.
TURN 105 107 {ECO:0000244|PDB:3KSN}.
HELIX 110 116 {ECO:0000244|PDB:1IWL}.
HELIX 119 122 {ECO:0000244|PDB:1IWL}.
STRAND 125 130 {ECO:0000244|PDB:1IWL}.
STRAND 133 142 {ECO:0000244|PDB:1IWL}.
STRAND 144 152 {ECO:0000244|PDB:1IWL}.
STRAND 158 165 {ECO:0000244|PDB:1IWL}.
STRAND 170 181 {ECO:0000244|PDB:1IWL}.
HELIX 185 188 {ECO:0000244|PDB:1IWL}.
STRAND 197 200 {ECO:0000244|PDB:1IWL}.
SEQUENCE 203 AA; 22497 MW; F2884D82D8DFEF1D CRC64;
MKKIAITCAL LSSLVASSVW ADAASDLKSR LDKVSSFHAS FTQKVTDGSG AAVQEGQGDL
WVKRPNLFNW HMTQPDESIL VSDGKTLWFY NPFVEQATAT WLKDATGNTP FMLIARNQSS
DWQQYNIKQN GDDFVLTPKA SNGNLKQFTI NVGRDGTIHQ FSAVEQDDQR SSYQLKSQQN
GAVDAAKFTF TPPQGVTVDD QRK


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