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Multidrug efflux pump subunit AcrB (AcrAB-TolC multidrug efflux pump subunit AcrB) (Acridine resistance protein B)

 ACRB_ECOLI              Reviewed;        1049 AA.
P31224; Q2MBW5;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
07-NOV-2018, entry version 173.
RecName: Full=Multidrug efflux pump subunit AcrB;
AltName: Full=AcrAB-TolC multidrug efflux pump subunit AcrB;
AltName: Full=Acridine resistance protein B;
Name=acrB; Synonyms=acrE; OrderedLocusNames=b0462, JW0451;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Xu J., Bertrand K.P.;
"Nucleotide sequence of the acrAB operon from Escherichia coli.";
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W4573;
PubMed=8407802; DOI=10.1128/jb.175.19.6299-6313.1993;
Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.;
"Molecular cloning and characterization of acrA and acrE genes of
Escherichia coli.";
J. Bacteriol. 175:6299-6313(1993).
[3]
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.
[4]
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).
[5]
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).
[6]
CHARACTERIZATION.
PubMed=7651136; DOI=10.1111/j.1365-2958.1995.tb02390.x;
Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.;
"Genes acrA and acrB encode a stress-induced efflux system of
Escherichia coli.";
Mol. Microbiol. 16:45-55(1995).
[7]
INTERACTION WITH ACRA.
PubMed=10920254; DOI=10.1093/oxfordjournals.jbchem.a022741;
Kawabe T., Fujihira E., Yamaguchi A.;
"Molecular construction of a multidrug exporter system, AcrAB:
molecular interaction between AcrA and AcrB, and cleavage of the N-
terminal signal sequence of AcrA.";
J. Biochem. 128:195-200(2000).
[8]
INTERACTION WITH ACRA AND TOLC, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=15228545; DOI=10.1111/j.1365-2958.2004.04158.x;
Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.;
"Interactions underlying assembly of the Escherichia coli AcrAB-TolC
multidrug efflux system.";
Mol. Microbiol. 53:697-706(2004).
[9]
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).
[10]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100;
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).
[12]
FUNCTION, INTERACTION WITH ACRZ, SUBUNIT, INDUCTION, AND MUTAGENESIS
OF HIS-526.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=23010927; DOI=10.1073/pnas.1210093109;
Hobbs E.C., Yin X., Paul B.J., Astarita J.L., Storz G.;
"Conserved small protein associates with the multidrug efflux pump
AcrB and differentially affects antibiotic resistance.";
Proc. Natl. Acad. Sci. U.S.A. 109:16696-16701(2012).
[13]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), AND SUBUNIT.
PubMed=12374972; DOI=10.1038/nature01050;
Murakami S., Nakashima R., Yamashita E., Yamaguchi A.;
"Crystal structure of bacterial multidrug efflux transporter AcrB.";
Nature 419:587-593(2002).
[14]
X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES,
AND SUBUNIT.
PubMed=12738864; DOI=10.1126/science.1083137;
Yu E.W., McDermott G., Zgurskaya H.I., Nikaido H., Koshland D.E. Jr.;
"Structural basis of multiple drug-binding capacity of the AcrB
multidrug efflux pump.";
Science 300:976-980(2003).
[15]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE,
SUBUNIT, AND FUNCTION.
PubMed=16915237; DOI=10.1038/nature05076;
Murakami S., Nakashima R., Yamashita E., Matsumoto T., Yamaguchi A.;
"Crystal structures of a multidrug transporter reveal a functionally
rotating mechanism.";
Nature 443:173-179(2006).
[16]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, AND FUNCTION.
PubMed=16946072; DOI=10.1126/science.1131542;
Seeger M.A., Schiefner A., Eicher T., Verrey F., Diederichs K.,
Pos K.M.;
"Structural asymmetry of AcrB trimer suggests a peristaltic pump
mechanism.";
Science 313:1295-1298(2006).
[17]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, AND SUBUNIT.
PubMed=17194213; DOI=10.1371/journal.pbio.0050007;
Sennhauser G., Amstutz P., Briand C., Storchenegger O., Gruetter M.G.;
"Drug export pathway of multidrug exporter AcrB revealed by DARPin
inhibitors.";
PLoS Biol. 5:107-113(2007).
-!- FUNCTION: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex
with broad substrate specificity that uses the proton motive force
to export substrates. {ECO:0000269|PubMed:16915237,
ECO:0000269|PubMed:16946072, ECO:0000269|PubMed:17194213,
ECO:0000269|PubMed:23010927}.
-!- FUNCTION: Involved in contact-dependent growth inhibition (CDI),
acts downstream of BamA, the receptor for CDI. Its role in CDI is
independent of the AcrA-AcrB-TolC efflux pump complex.
{ECO:0000269|PubMed:18761695}.
-!- SUBUNIT: Homotrimer, with large domains that extend into the
periplasm, interacts with AcrA and TolC. AcrA may be required to
stably link this protein and TolC. Interacts with AcrZ. Part of
the AcrA-AcrB-AcrZ-TolC efflux pump. {ECO:0000269|PubMed:10920254,
ECO:0000269|PubMed:12374972, ECO:0000269|PubMed:12738864,
ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137,
ECO:0000269|PubMed:16915237, ECO:0000269|PubMed:16946072,
ECO:0000269|PubMed:17194213, ECO:0000269|PubMed:23010927}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-551006, EBI-551006;
P0AAW9:acrZ; NbExp=7; IntAct=EBI-551006, EBI-6313593;
P0ADZ7:yajC; NbExp=2; IntAct=EBI-551006, EBI-1130723;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137}; Multi-
pass membrane protein {ECO:0000269|PubMed:15228545,
ECO:0000269|PubMed:16079137}.
-!- INDUCTION: Positively regulated by MarA, Rob and SoxS
transcriptional regulators (at protein level).
{ECO:0000269|PubMed:23010927}.
-!- DISRUPTION PHENOTYPE: Loss of susceptibility to contact-dependent
growth inhibition (CDI); inhibiting cells still contact the
target. {ECO:0000269|PubMed:18761695}.
-!- SIMILARITY: Belongs to the resistance-nodulation-cell division
(RND) (TC 2.A.6) family. {ECO:0000305}.
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EMBL; M94248; AAA23411.1; -; Genomic_DNA.
EMBL; U00734; AAA67135.1; -; Genomic_DNA.
EMBL; U82664; AAB40216.1; -; Genomic_DNA.
EMBL; U00096; AAC73564.1; -; Genomic_DNA.
EMBL; AP009048; BAE76241.1; -; Genomic_DNA.
PIR; B36938; B36938.
RefSeq; NP_414995.1; NC_000913.3.
RefSeq; WP_001132469.1; NZ_LN832404.1.
PDB; 1IWG; X-ray; 3.50 A; A=1-1049.
PDB; 1OY6; X-ray; 3.68 A; A=1-1049.
PDB; 1OY8; X-ray; 3.63 A; A=1-1049.
PDB; 1OY9; X-ray; 3.80 A; A=1-1049.
PDB; 1OYD; X-ray; 3.80 A; A=1-1049.
PDB; 1OYE; X-ray; 3.48 A; A=1-1049.
PDB; 1T9T; X-ray; 3.23 A; A=1-1049.
PDB; 1T9U; X-ray; 3.11 A; A=1-1049.
PDB; 1T9V; X-ray; 3.80 A; A=1-1049.
PDB; 1T9W; X-ray; 3.23 A; A=1-1049.
PDB; 1T9X; X-ray; 3.08 A; A=1-1049.
PDB; 1T9Y; X-ray; 3.64 A; A=1-1049.
PDB; 2DHH; X-ray; 2.80 A; A/B/C=1-1049.
PDB; 2DR6; X-ray; 3.30 A; A/B/C=1-1049.
PDB; 2DRD; X-ray; 3.10 A; A/B/C=1-1049.
PDB; 2GIF; X-ray; 2.90 A; A/B/C=1-1049.
PDB; 2HQC; X-ray; 3.56 A; A=1-1049.
PDB; 2HQD; X-ray; 3.65 A; A=1-1049.
PDB; 2HQF; X-ray; 3.38 A; A=1-1049.
PDB; 2HQG; X-ray; 3.38 A; A=1-1049.
PDB; 2HRT; X-ray; 3.00 A; A/B/C/D/E/F=1-1049.
PDB; 2I6W; X-ray; 3.10 A; A=1-1049.
PDB; 2J8S; X-ray; 2.54 A; A/B/C=1-1049.
PDB; 2RDD; X-ray; 3.50 A; A=1-1049.
PDB; 2W1B; X-ray; 3.85 A; A=1-1049.
PDB; 3AOA; X-ray; 3.35 A; A/B/C=1-1049.
PDB; 3AOB; X-ray; 3.35 A; A/B/C=1-1049.
PDB; 3AOC; X-ray; 3.34 A; A/B/C=1-1049.
PDB; 3AOD; X-ray; 3.30 A; A/B/C=1-1049.
PDB; 3D9B; X-ray; 3.42 A; A=1-1049.
PDB; 3NOC; X-ray; 2.70 A; A/B/C=1-1049.
PDB; 3NOG; X-ray; 3.34 A; A/B/C=1-1049.
PDB; 3W9H; X-ray; 3.05 A; A/B/C=1-1033.
PDB; 4C48; X-ray; 3.30 A; A=1-1047.
PDB; 4CDI; X-ray; 3.70 A; A=1-1049.
PDB; 4DX5; X-ray; 1.90 A; A/B/C=1-1049.
PDB; 4DX6; X-ray; 2.90 A; A/B/C=1-1049.
PDB; 4DX7; X-ray; 2.25 A; A/B/C=1-1049.
PDB; 4K7Q; X-ray; 3.50 A; A=1-1049.
PDB; 4U8V; X-ray; 2.30 A; A/B/C=1-1049.
PDB; 4U8Y; X-ray; 2.10 A; A/B/C=1-1049.
PDB; 4U95; X-ray; 2.00 A; A/B/C=1-1049.
PDB; 4U96; X-ray; 2.20 A; A/B/C=1-1049.
PDB; 4ZIT; X-ray; 3.30 A; A/B/C/D/E/F=1-1049.
PDB; 4ZIV; X-ray; 3.16 A; A/B/C/D/E/F=1-1049.
PDB; 4ZIW; X-ray; 3.40 A; A/B/C/D/E/F=1-1049.
PDB; 4ZJL; X-ray; 3.47 A; A/B/C/D/E/F=1-1049.
PDB; 4ZJO; X-ray; 3.60 A; A/B/C/D/E/F=1-1049.
PDB; 4ZJQ; X-ray; 3.59 A; A/B/C/D/E/F=1-1049.
PDB; 4ZLJ; X-ray; 3.26 A; A=1-1049.
PDB; 4ZLL; X-ray; 3.36 A; A=1-1049.
PDB; 4ZLN; X-ray; 3.56 A; A=1-1049.
PDB; 5EN5; X-ray; 2.30 A; A/B/C=39-329, A/B/C=561-869.
PDB; 5ENO; X-ray; 2.20 A; A/B/C=39-329, A/B/C=561-869.
PDB; 5ENP; X-ray; 1.90 A; A/B/C=39-329, A/B/C=561-869.
PDB; 5ENQ; X-ray; 1.80 A; A/B/C=39-329, A/B/C=561-869.
PDB; 5ENR; X-ray; 2.30 A; A/B/C=39-329, A/B/C=561-869.
PDB; 5ENS; X-ray; 2.80 A; A/B/C=39-329, A/B/C=561-869.
PDB; 5ENT; X-ray; 2.50 A; A/B/C=39-329, A/B/C=561-869.
PDB; 5JMN; X-ray; 2.50 A; A/B/C=1-1049.
PDB; 5NC5; X-ray; 3.20 A; A/B/C=1-1049.
PDB; 5NG5; EM; 6.50 A; J/K/L=1-1049.
PDB; 5O66; EM; 5.90 A; J/K/L=1-1049.
PDB; 5V5S; EM; 6.50 A; J/K/L=1-1049.
PDB; 5YIL; X-ray; 3.00 A; A/B/C=1-1049.
PDBsum; 1IWG; -.
PDBsum; 1OY6; -.
PDBsum; 1OY8; -.
PDBsum; 1OY9; -.
PDBsum; 1OYD; -.
PDBsum; 1OYE; -.
PDBsum; 1T9T; -.
PDBsum; 1T9U; -.
PDBsum; 1T9V; -.
PDBsum; 1T9W; -.
PDBsum; 1T9X; -.
PDBsum; 1T9Y; -.
PDBsum; 2DHH; -.
PDBsum; 2DR6; -.
PDBsum; 2DRD; -.
PDBsum; 2GIF; -.
PDBsum; 2HQC; -.
PDBsum; 2HQD; -.
PDBsum; 2HQF; -.
PDBsum; 2HQG; -.
PDBsum; 2HRT; -.
PDBsum; 2I6W; -.
PDBsum; 2J8S; -.
PDBsum; 2RDD; -.
PDBsum; 2W1B; -.
PDBsum; 3AOA; -.
PDBsum; 3AOB; -.
PDBsum; 3AOC; -.
PDBsum; 3AOD; -.
PDBsum; 3D9B; -.
PDBsum; 3NOC; -.
PDBsum; 3NOG; -.
PDBsum; 3W9H; -.
PDBsum; 4C48; -.
PDBsum; 4CDI; -.
PDBsum; 4DX5; -.
PDBsum; 4DX6; -.
PDBsum; 4DX7; -.
PDBsum; 4K7Q; -.
PDBsum; 4U8V; -.
PDBsum; 4U8Y; -.
PDBsum; 4U95; -.
PDBsum; 4U96; -.
PDBsum; 4ZIT; -.
PDBsum; 4ZIV; -.
PDBsum; 4ZIW; -.
PDBsum; 4ZJL; -.
PDBsum; 4ZJO; -.
PDBsum; 4ZJQ; -.
PDBsum; 4ZLJ; -.
PDBsum; 4ZLL; -.
PDBsum; 4ZLN; -.
PDBsum; 5EN5; -.
PDBsum; 5ENO; -.
PDBsum; 5ENP; -.
PDBsum; 5ENQ; -.
PDBsum; 5ENR; -.
PDBsum; 5ENS; -.
PDBsum; 5ENT; -.
PDBsum; 5JMN; -.
PDBsum; 5NC5; -.
PDBsum; 5NG5; -.
PDBsum; 5O66; -.
PDBsum; 5V5S; -.
PDBsum; 5YIL; -.
ProteinModelPortal; P31224; -.
SMR; P31224; -.
BioGrid; 4259859; 386.
DIP; DIP-9049N; -.
IntAct; P31224; 9.
MINT; P31224; -.
STRING; 316385.ECDH10B_0418; -.
ChEMBL; CHEMBL1681614; -.
DrugBank; DB03619; Deoxycholic Acid.
DrugBank; DB04209; Dequadin.
DrugBank; DB03825; Rhodamine 6G.
TCDB; 2.A.6.2.2; the resistance-nodulation-cell division (rnd) superfamily.
EPD; P31224; -.
PaxDb; P31224; -.
PRIDE; P31224; -.
EnsemblBacteria; AAC73564; AAC73564; b0462.
EnsemblBacteria; BAE76241; BAE76241; BAE76241.
GeneID; 945108; -.
KEGG; ecj:JW0451; -.
KEGG; eco:b0462; -.
PATRIC; fig|1411691.4.peg.1814; -.
EchoBASE; EB1655; -.
EcoGene; EG11704; acrB.
eggNOG; ENOG4105BZS; Bacteria.
eggNOG; COG0841; LUCA.
HOGENOM; HOG000158129; -.
InParanoid; P31224; -.
KO; K18138; -.
PhylomeDB; P31224; -.
BioCyc; EcoCyc:ACRB-MONOMER; -.
BioCyc; MetaCyc:ACRB-MONOMER; -.
EvolutionaryTrace; P31224; -.
PRO; PR:P31224; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:1990281; C:efflux pump complex; IPI:EcoCyc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0015238; F:drug transmembrane transporter activity; IMP:EcoCyc.
GO; GO:0015307; F:drug:proton antiporter activity; IDA:EcoCyc.
GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006855; P:drug transmembrane transport; IMP:EcoCyc.
GO; GO:0042493; P:response to drug; IMP:EcoCyc.
Gene3D; 3.30.2090.10; -; 2.
InterPro; IPR027463; AcrB_DN_DC_subdom.
InterPro; IPR001036; Acrflvin-R.
InterPro; IPR004764; HAE1.
PANTHER; PTHR32063; PTHR32063; 1.
Pfam; PF00873; ACR_tran; 1.
PRINTS; PR00702; ACRIFLAVINRP.
SUPFAM; SSF82714; SSF82714; 2.
TIGRFAMs; TIGR00915; 2A0602; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Membrane; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1049 Multidrug efflux pump subunit AcrB.
/FTId=PRO_0000161811.
TOPO_DOM 1 9 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 10 28 Helical; Name=1.
TOPO_DOM 29 336 Periplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 337 356 Helical; Name=2.
TOPO_DOM 357 365 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 366 385 Helical; Name=3.
TOPO_DOM 386 391 Periplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 392 413 Helical; Name=4.
TOPO_DOM 414 438 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 439 457 Helical; Name=5.
TOPO_DOM 458 465 Periplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 466 490 Helical; Name=6.
TOPO_DOM 491 538 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 539 555 Helical; Name=7.
TOPO_DOM 556 871 Periplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 872 888 Helical; Name=8.
TOPO_DOM 889 898 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 899 918 Helical; Name=9.
TOPO_DOM 919 924 Periplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 925 943 Helical; Name=10.
TOPO_DOM 944 972 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 973 992 Helical; Name=11.
TOPO_DOM 993 998 Periplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 999 1018 Helical; Name=12.
TOPO_DOM 1019 1049 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
MUTAGEN 526 526 H->Y: Partially restores chloramphenicol
resistance to an AcrZ G30R mutant.
{ECO:0000269|PubMed:23010927}.
HELIX 2 6 {ECO:0000244|PDB:4DX5}.
HELIX 9 29 {ECO:0000244|PDB:4DX5}.
STRAND 32 35 {ECO:0000244|PDB:2GIF}.
STRAND 42 48 {ECO:0000244|PDB:5ENQ}.
HELIX 54 60 {ECO:0000244|PDB:5ENQ}.
HELIX 62 66 {ECO:0000244|PDB:5ENQ}.
STRAND 75 83 {ECO:0000244|PDB:5ENQ}.
STRAND 86 94 {ECO:0000244|PDB:5ENQ}.
STRAND 95 97 {ECO:0000244|PDB:2DR6}.
HELIX 100 114 {ECO:0000244|PDB:5ENQ}.
HELIX 115 117 {ECO:0000244|PDB:5ENQ}.
HELIX 120 123 {ECO:0000244|PDB:5ENQ}.
STRAND 128 130 {ECO:0000244|PDB:5ENQ}.
STRAND 132 144 {ECO:0000244|PDB:5ENQ}.
STRAND 145 147 {ECO:0000244|PDB:3W9H}.
HELIX 151 161 {ECO:0000244|PDB:5ENQ}.
HELIX 163 168 {ECO:0000244|PDB:5ENQ}.
TURN 169 171 {ECO:0000244|PDB:1T9X}.
STRAND 172 179 {ECO:0000244|PDB:5ENQ}.
STRAND 182 188 {ECO:0000244|PDB:5ENQ}.
HELIX 190 195 {ECO:0000244|PDB:5ENQ}.
HELIX 200 210 {ECO:0000244|PDB:5ENQ}.
STRAND 215 220 {ECO:0000244|PDB:5ENQ}.
STRAND 232 235 {ECO:0000244|PDB:5ENQ}.
HELIX 243 247 {ECO:0000244|PDB:5ENQ}.
STRAND 250 253 {ECO:0000244|PDB:5ENQ}.
TURN 255 257 {ECO:0000244|PDB:2DHH}.
STRAND 259 261 {ECO:0000244|PDB:5ENQ}.
HELIX 262 264 {ECO:0000244|PDB:5ENQ}.
STRAND 266 273 {ECO:0000244|PDB:5ENQ}.
STRAND 278 281 {ECO:0000244|PDB:5ENQ}.
STRAND 284 294 {ECO:0000244|PDB:5ENQ}.
STRAND 295 298 {ECO:0000244|PDB:2DHH}.
HELIX 299 313 {ECO:0000244|PDB:5ENQ}.
HELIX 314 316 {ECO:0000244|PDB:5ENQ}.
STRAND 317 319 {ECO:0000244|PDB:2DHH}.
STRAND 321 328 {ECO:0000244|PDB:5ENQ}.
HELIX 330 359 {ECO:0000244|PDB:4DX5}.
HELIX 362 385 {ECO:0000244|PDB:4DX5}.
HELIX 392 423 {ECO:0000244|PDB:4DX5}.
HELIX 427 453 {ECO:0000244|PDB:4DX5}.
HELIX 455 458 {ECO:0000244|PDB:4DX5}.
HELIX 461 496 {ECO:0000244|PDB:4DX5}.
TURN 505 508 {ECO:0000244|PDB:2GIF}.
STRAND 509 511 {ECO:0000244|PDB:4ZIW}.
HELIX 512 536 {ECO:0000244|PDB:4DX5}.
STRAND 537 539 {ECO:0000244|PDB:3NOG}.
HELIX 540 558 {ECO:0000244|PDB:4DX5}.
STRAND 561 564 {ECO:0000244|PDB:2DR6}.
STRAND 571 577 {ECO:0000244|PDB:5ENQ}.
HELIX 584 599 {ECO:0000244|PDB:5ENQ}.
TURN 600 605 {ECO:0000244|PDB:5ENQ}.
STRAND 606 616 {ECO:0000244|PDB:5ENQ}.
STRAND 619 631 {ECO:0000244|PDB:5ENQ}.
HELIX 634 636 {ECO:0000244|PDB:5ENQ}.
HELIX 640 642 {ECO:0000244|PDB:5ENQ}.
HELIX 644 655 {ECO:0000244|PDB:5ENQ}.
STRAND 658 660 {ECO:0000244|PDB:3NOC}.
STRAND 662 666 {ECO:0000244|PDB:5ENQ}.
HELIX 672 674 {ECO:0000244|PDB:4DX5}.
STRAND 679 686 {ECO:0000244|PDB:5ENQ}.
HELIX 692 707 {ECO:0000244|PDB:5ENQ}.
TURN 710 712 {ECO:0000244|PDB:5ENQ}.
STRAND 713 720 {ECO:0000244|PDB:5ENQ}.
STRAND 724 731 {ECO:0000244|PDB:5ENQ}.
HELIX 733 739 {ECO:0000244|PDB:5ENQ}.
HELIX 743 755 {ECO:0000244|PDB:5ENQ}.
STRAND 757 764 {ECO:0000244|PDB:5ENQ}.
STRAND 767 775 {ECO:0000244|PDB:5ENQ}.
HELIX 777 779 {ECO:0000244|PDB:5ENQ}.
STRAND 780 782 {ECO:0000244|PDB:5ENQ}.
HELIX 783 788 {ECO:0000244|PDB:5ENQ}.
STRAND 790 792 {ECO:0000244|PDB:5ENQ}.
STRAND 794 796 {ECO:0000244|PDB:3NOC}.
STRAND 798 800 {ECO:0000244|PDB:5ENQ}.
HELIX 801 803 {ECO:0000244|PDB:5ENQ}.
STRAND 804 812 {ECO:0000244|PDB:5ENQ}.
STRAND 814 819 {ECO:0000244|PDB:5ENQ}.
STRAND 822 831 {ECO:0000244|PDB:5ENQ}.
STRAND 833 835 {ECO:0000244|PDB:3NOC}.
HELIX 837 848 {ECO:0000244|PDB:5ENQ}.
STRAND 855 859 {ECO:0000244|PDB:5ENQ}.
HELIX 861 863 {ECO:0000244|PDB:5ENQ}.
STRAND 865 868 {ECO:0000244|PDB:4DX5}.
TURN 869 871 {ECO:0000244|PDB:1T9W}.
HELIX 873 892 {ECO:0000244|PDB:4DX5}.
STRAND 894 897 {ECO:0000244|PDB:5YIL}.
HELIX 898 902 {ECO:0000244|PDB:4DX5}.
HELIX 905 919 {ECO:0000244|PDB:4DX5}.
HELIX 925 954 {ECO:0000244|PDB:4DX5}.
TURN 955 957 {ECO:0000244|PDB:4C48}.
HELIX 960 985 {ECO:0000244|PDB:4DX5}.
HELIX 987 990 {ECO:0000244|PDB:4DX5}.
STRAND 994 996 {ECO:0000244|PDB:2J8S}.
HELIX 997 1032 {ECO:0000244|PDB:4DX5}.
TURN 1033 1035 {ECO:0000244|PDB:4K7Q}.
STRAND 1036 1038 {ECO:0000244|PDB:2GIF}.
STRAND 1039 1041 {ECO:0000244|PDB:2J8S}.
SEQUENCE 1049 AA; 113574 MW; 19670E3C4CC29055 CRC64;
MPNFFIDRPI FAWVIAIIIM LAGGLAILKL PVAQYPTIAP PAVTISASYP GADAKTVQDT
VTQVIEQNMN GIDNLMYMSS NSDSTGTVQI TLTFESGTDA DIAQVQVQNK LQLAMPLLPQ
EVQQQGVSVE KSSSSFLMVV GVINTDGTMT QEDISDYVAA NMKDAISRTS GVGDVQLFGS
QYAMRIWMNP NELNKFQLTP VDVITAIKAQ NAQVAAGQLG GTPPVKGQQL NASIIAQTRL
TSTEEFGKIL LKVNQDGSRV LLRDVAKIEL GGENYDIIAE FNGQPASGLG IKLATGANAL
DTAAAIRAEL AKMEPFFPSG LKIVYPYDTT PFVKISIHEV VKTLVEAIIL VFLVMYLFLQ
NFRATLIPTI AVPVVLLGTF AVLAAFGFSI NTLTMFGMVL AIGLLVDDAI VVVENVERVM
AEEGLPPKEA TRKSMGQIQG ALVGIAMVLS AVFVPMAFFG GSTGAIYRQF SITIVSAMAL
SVLVALILTP ALCATMLKPI AKGDHGEGKK GFFGWFNRMF EKSTHHYTDS VGGILRSTGR
YLVLYLIIVV GMAYLFVRLP SSFLPDEDQG VFMTMVQLPA GATQERTQKV LNEVTHYYLT
KEKNNVESVF AVNGFGFAGR GQNTGIAFVS LKDWADRPGE ENKVEAITMR ATRAFSQIKD
AMVFAFNLPA IVELGTATGF DFELIDQAGL GHEKLTQARN QLLAEAAKHP DMLTSVRPNG
LEDTPQFKID IDQEKAQALG VSINDINTTL GAAWGGSYVN DFIDRGRVKK VYVMSEAKYR
MLPDDIGDWY VRAADGQMVP FSAFSSSRWE YGSPRLERYN GLPSMEILGQ AAPGKSTGEA
MELMEQLASK LPTGVGYDWT GMSYQERLSG NQAPSLYAIS LIVVFLCLAA LYESWSIPFS
VMLVVPLGVI GALLAATFRG LTNDVYFQVG LLTTIGLSAK NAILIVEFAK DLMDKEGKGL
IEATLDAVRM RLRPILMTSL AFILGVMPLV ISTGAGSGAQ NAVGTGVMGG MVTATVLAIF
FVPVFFVVVR RRFSRKNEDI EHSHTVDHH


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