BAMA_ECOLI
ID BAMA_ECOLI Reviewed; 810 AA.
AC P0A940; P39170; P39181; P77465; Q548B8; Q8KR94; Q9R2E3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Outer membrane protein assembly factor BamA {ECO:0000255|HAMAP-Rule:MF_01430};
DE AltName: Full=Omp85;
DE Flags: Precursor;
GN Name=bamA {ECO:0000255|HAMAP-Rule:MF_01430}; Synonyms=yaeT, yzzN, yzzY;
GN OrderedLocusNames=b0177, JW0172;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11274153; DOI=10.1074/jbc.m100464200;
RA Dartigalongue C., Missiakas D., Raina S.;
RT "Characterization of the Escherichia coli sigma E regulon.";
RL J. Biol. Chem. 276:20866-20875(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RA Allison H.E., Sergeant M.J., Cookson S.S., Yaxian Y., James C.E.,
RA Sharp R.J., Saunders J.R., McCarthy A.J.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PROTEIN SEQUENCE OF 21-32 AND 351-362.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP POTRA DOMAIN.
RX PubMed=14559180; DOI=10.1016/j.tibs.2003.08.003;
RA Sanchez-Pulido L., Devos D., Genevrois S., Vicente M., Valencia A.;
RT "POTRA: a conserved domain in the FtsQ family and a class of beta-barrel
RT outer membrane proteins.";
RL Trends Biochem. Sci. 28:523-526(2003).
RN [9]
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=15851030; DOI=10.1016/j.cell.2005.02.015;
RA Wu T., Malinverni J., Ruiz N., Kim S., Silhavy T.J., Kahne D.;
RT "Identification of a multicomponent complex required for outer membrane
RT biogenesis in Escherichia coli.";
RL Cell 121:235-245(2005).
RN [10]
RP FUNCTION.
RX PubMed=15951436; DOI=10.1074/jbc.m504796200;
RA Doerrler W.T., Raetz C.R.H.;
RT "Loss of outer membrane proteins without inhibition of lipid export in an
RT Escherichia coli YaeT mutant.";
RL J. Biol. Chem. 280:27679-27687(2005).
RN [11]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16102012; DOI=10.1111/j.1365-2958.2005.04775.x;
RA Werner J., Misra R.;
RT "YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent
RT outer membrane proteins of Escherichia coli.";
RL Mol. Microbiol. 57:1450-1459(2005).
RN [13]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH BAMB AND BAMD.
RC STRAIN=K12;
RX PubMed=16824102; DOI=10.1111/j.1365-2958.2006.05211.x;
RA Malinverni J.C., Werner J., Kim S., Sklar J.G., Kahne D., Misra R.,
RA Silhavy T.J.;
RT "YfiO stabilizes the YaeT complex and is essential for outer membrane
RT protein assembly in Escherichia coli.";
RL Mol. Microbiol. 61:151-164(2006).
RN [14]
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=17404237; DOI=10.1073/pnas.0701579104;
RA Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D.,
RA Silhavy T.J.;
RT "Lipoprotein SmpA is a component of the YaeT complex that assembles outer
RT membrane proteins in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:6400-6405(2007).
RN [15]
RP FUNCTION IN CDI (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061;
RX PubMed=18761695; DOI=10.1111/j.1365-2958.2008.06404.x;
RA Aoki S.K., Malinverni J.C., Jacoby K., Thomas B., Pamma R., Trinh B.N.,
RA Remers S., Webb J., Braaten B.A., Silhavy T.J., Low D.A.;
RT "Contact-dependent growth inhibition requires the essential outer membrane
RT protein BamA (YaeT) as the receptor and the inner membrane transport
RT protein AcrB.";
RL Mol. Microbiol. 70:323-340(2008).
RN [16]
RP FUNCTION, AND SUBUNIT.
RX PubMed=20378773; DOI=10.1126/science.1188919;
RA Hagan C.L., Kim S., Kahne D.;
RT "Reconstitution of outer membrane protein assembly from purified
RT components.";
RL Science 328:890-892(2010).
RN [17]
RP FUNCTION, AND SUBUNIT.
RX PubMed=21823654; DOI=10.1021/bi2010784;
RA Hagan C.L., Kahne D.;
RT "The reconstituted Escherichia coli Bam complex catalyzes multiple rounds
RT of beta-barrel assembly.";
RL Biochemistry 50:7444-7446(2011).
RN [18]
RP INTERACTION WITH BAMB AND BAMD.
RX PubMed=21586578; DOI=10.1074/jbc.m111.238931;
RA Albrecht R., Zeth K.;
RT "Structural basis of outer membrane protein biogenesis in bacteria.";
RL J. Biol. Chem. 286:27792-27803(2011).
RN [19]
RP FUNCTION IN CDI (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=23469034; DOI=10.1371/journal.pone.0057609;
RA Webb J.S., Nikolakakis K.C., Willett J.L., Aoki S.K., Hayes C.S., Low D.A.;
RT "Delivery of CdiA nuclease toxins into target cells during contact-
RT dependent growth inhibition.";
RL PLoS ONE 8:E57609-E57609(2013).
RN [20]
RP FUNCTION IN CDI (MICROBIAL INFECTION), STRAIN SPECIFICITY, SUBCELLULAR
RP LOCATION, TOPOLOGY, AND MUTAGENESIS OF 554-GLU--ASP-562; 556-PRO--SER-564;
RP 675-PHE--SER-702; 677-HIS--ASP-685 AND 754-TYR-SER-755.
RX PubMed=23882017; DOI=10.1128/mbio.00480-13;
RA Ruhe Z.C., Wallace A.B., Low D.A., Hayes C.S.;
RT "Receptor polymorphism restricts contact-dependent growth inhibition to
RT members of the same species.";
RL MBio 4:E00480-E00480(2013).
RN [21] {ECO:0007744|PDB:2QCZ, ECO:0007744|PDB:2QDF}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 21-351, AND DOMAIN.
RX PubMed=17702946; DOI=10.1126/science.1143993;
RA Kim S., Malinverni J.C., Sliz P., Silhavy T.J., Harrison S.C., Kahne D.;
RT "Structure and function of an essential component of the outer membrane
RT protein assembly machine.";
RL Science 317:961-964(2007).
RN [22] {ECO:0007744|PDB:2V9H}
RP STRUCTURE BY NMR OF 21-184, AND DOMAIN.
RX PubMed=18430136; DOI=10.1111/j.1365-2958.2008.06225.x;
RA Knowles T.J., Jeeves M., Bobat S., Dancea F., McClelland D., Palmer T.,
RA Overduin M., Henderson I.R.;
RT "Fold and function of polypeptide transport-associated domains responsible
RT for delivering unfolded proteins to membranes.";
RL Mol. Microbiol. 68:1216-1227(2008).
RN [23] {ECO:0007744|PDB:3EFC}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 21-410, AND DOMAIN.
RX PubMed=19081063; DOI=10.1016/j.str.2008.09.014;
RA Gatzeva-Topalova P.Z., Walton T.A., Sousa M.C.;
RT "Crystal structure of YaeT: conformational flexibility and substrate
RT recognition.";
RL Structure 16:1873-1881(2008).
RN [24] {ECO:0007744|PDB:3Q6B}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 266-420, AND DOMAIN.
RX PubMed=21795783; DOI=10.1107/s1744309111014254;
RA Zhang H., Gao Z.Q., Hou H.F., Xu J.H., Li L.F., Su X.D., Dong Y.H.;
RT "High-resolution structure of a new crystal form of BamA POTRA4-5 from
RT Escherichia coli.";
RL Acta Crystallogr. F 67:734-738(2011).
RN [25] {ECO:0007744|PDB:4C4V}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 347-810 AND 344-810, SUBCELLULAR
RP LOCATION, DOMAIN, AND TOPOLOGY.
RC STRAIN=BL21 (DE3);
RX PubMed=24914988; DOI=10.1107/s1399004714007482;
RA Albrecht R., Schutz M., Oberhettinger P., Faulstich M., Bermejo I.,
RA Rudel T., Diederichs K., Zeth K.;
RT "Structure of BamA, an essential factor in outer membrane protein
RT biogenesis.";
RL Acta Crystallogr. D 70:1779-1789(2014).
RN [26] {ECO:0007744|PDB:4N75}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 427-810, SUBCELLULAR LOCATION,
RP DOMAIN, TOPOLOGY, AND MUTAGENESIS OF GLU-435; ASP-464; ASP-500; ARG-547;
RP ARG-661; 673-VAL--SER-702; ASP-740 AND GLU-800.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24619089; DOI=10.1096/fj.13-248450;
RA Ni D., Wang Y., Yang X., Zhou H., Hou X., Cao B., Lu Z., Zhao X., Yang K.,
RA Huang Y.;
RT "Structural and functional analysis of the beta-barrel domain of BamA from
RT Escherichia coli.";
RL FASEB J. 28:2677-2685(2014).
RN [27] {ECO:0007744|PDB:5LJO}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 24-806 IN LATERAL OPEN
RP BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, AND
RP MUTAGENESIS OF ILE-430 AND LYS-808.
RX PubMed=27686148; DOI=10.1038/ncomms12865;
RA Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N., Brockwell D.J.,
RA Ashcroft A.E., Radford S.E., Ranson N.A.;
RT "Lateral opening in the intact beta-barrel assembly machinery captured by
RT cryo-EM.";
RL Nat. Commun. 7:12865-12865(2016).
RN [28] {ECO:0007744|PDB:5AYW}
RP X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 22-810 IN LATERAL CLOSED BAM
RP COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-181;
RP LYS-251; ASN-259 AND GLY-429.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=26900875; DOI=10.1038/nsmb.3181;
RA Han L., Zheng J., Wang Y., Yang X., Liu Y., Sun C., Cao B., Zhou H., Ni D.,
RA Lou J., Zhao Y., Huang Y.;
RT "Structure of the BAM complex and its implications for biogenesis of outer-
RT membrane proteins.";
RL Nat. Struct. Mol. Biol. 23:192-196(2016).
RN [29] {ECO:0007744|PDB:5D0O, ECO:0007744|PDB:5D0Q}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX AND
RP LATERAL OPEN BAMACDE SUBCOMPLEX, REACTION MECHANISM, SUBUNIT, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 351-LYS--LYS-353; LYS-351; ARG-366; GLU-373;
RP GLY-393; 415-VAL--LYS-419; 415-VAL--LYS-417; 417-LYS--LYS-419; GLU-435;
RP GLY-584 AND SER-658.
RX PubMed=26901871; DOI=10.1038/nature17199;
RA Gu Y., Li H., Dong H., Zeng Y., Zhang Z., Paterson N.G., Stansfeld P.J.,
RA Wang Z., Zhang Y., Wang W., Dong C.;
RT "Structural basis of outer membrane protein insertion by the BAM complex.";
RL Nature 531:64-69(2016).
RN [30] {ECO:0007744|PDB:5EKQ}
RP X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 21-810 OF LATERAL OPEN BAMACDE
RP SUBCOMPLEX, AND SUBUNIT.
RX PubMed=26744406; DOI=10.1126/science.aad3460;
RA Bakelar J., Buchanan S.K., Noinaj N.;
RT "The structure of the beta-barrel assembly machinery complex.";
RL Science 351:180-186(2016).
CC -!- FUNCTION: Part of the outer membrane protein assembly complex (Bam),
CC which is involved in assembly and insertion of beta-barrel proteins
CC into the outer membrane. Constitutes, with BamD, the core component of
CC the assembly machinery. Efficient substrate folding and insertion into
CC the outer membrane requires all 5 subunits (PubMed:20378773,
CC PubMed:21823654, PubMed:27686148). A lateral gate may open between the
CC first and last strands of the BamA beta-barrel that allows substrate to
CC insert into the outer membrane; comparison of the structures of
CC complete and nearly complete Bam complexes show there is considerable
CC movement of all 5 proteins (PubMed:27686148, PubMed:26900875,
CC PubMed:26901871, PubMed:26744406). {ECO:0000269|PubMed:15951436,
CC ECO:0000269|PubMed:16102012, ECO:0000269|PubMed:16824102,
CC ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21823654,
CC ECO:0000269|PubMed:26744406, ECO:0000269|PubMed:26900875,
CC ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:27686148}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for CdiA-EC93, the
CC contact-dependent growth inhibition (CDI) effector of E.coli strain
CC EC93; antibodies against extracellular epitopes decrease CDI. Its role
CC in CDI is independent of the other Bam complex components
CC (PubMed:18761695). Is not the receptor for CdiA from E.coli strain 536
CC / UPEC, which does not have the same mode of toxicity as CdiA from
CC strain EC93; the decreased expression of bamA101 in some experiments
CC decreases the level of outer membrane proteins in general
CC (PubMed:23469034, PubMed:23882017). Susceptibility to CdiA-EC93 is
CC dependent on E.coli BamA; replacing BamA with the gene from
CC S.typhimurium LT2, E.cloacae ATCC 13047 or D.dadantii 3937 renders
CC cells resistant to CdiA-EC93. Cells with BamA from another bacteria no
CC longer form CdiA-EC93-induced aggregates with EC93 cells. A chimera in
CC which E.cloacae extracellular loops 6 and 7 are replaced with loops 6
CC and 7 from E.coli is susceptible to CdiA-EC93 and to CdiA-CT from
CC strain 536 / UPEC (PubMed:23882017). {ECO:0000269|PubMed:18761695,
CC ECO:0000269|PubMed:23469034, ECO:0000269|PubMed:23882017}.
CC -!- SUBUNIT: Part of the Bam complex, which is composed of the outer
CC membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE.
CC BamA interacts directly with BamB and the BamCDE subcomplex. The Bam
CC complex has the shape of a hat, with the BamA beta-barrel crown in the
CC outer membrane and the periplasmic brim formed by the BamA POTRA
CC domains and the 4 lipoproteins (PubMed:27686148, PubMed:26900875,
CC PubMed:26901871, PubMed:26744406). {ECO:0000269|PubMed:15851030,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:16824102,
CC ECO:0000269|PubMed:17404237, ECO:0000269|PubMed:20378773,
CC ECO:0000269|PubMed:21586578, ECO:0000269|PubMed:21823654,
CC ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871,
CC ECO:0000269|PubMed:27686148}.
CC -!- INTERACTION:
CC P0A940; P77774: bamB; NbExp=23; IntAct=EBI-907371, EBI-907297;
CC P0A940; P0AC02: bamD; NbExp=26; IntAct=EBI-907371, EBI-1128087;
CC P0A940; P69411: rcsF; NbExp=3; IntAct=EBI-907371, EBI-1114706;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01430, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:23882017, ECO:0000269|PubMed:24619089,
CC ECO:0000269|PubMed:24914988, ECO:0000269|PubMed:26901871,
CC ECO:0000269|PubMed:9298646}.
CC -!- DOMAIN: Contains 5 N-terminal periplasmic polypeptide transport-
CC associated (POTRA) domains which interact with other subunits of the
CC complex, may recruit substrates from the periplasm into the outer
CC membrane and also act as a chaperone (PubMed:17702946, PubMed:18430136,
CC PubMed:19081063, PubMed:21795783, PubMed:14559180). The C-terminal
CC region forms a discontinuous 16-stranded beta-barrel transmembrane
CC region. The central pore is ellipsoid, and probably closed by
CC extracellular loop 6, perhaps with the aid of other loops
CC (PubMed:24914988, PubMed:24619089). {ECO:0000269|PubMed:17702946,
CC ECO:0000269|PubMed:18430136, ECO:0000269|PubMed:19081063,
CC ECO:0000269|PubMed:21795783, ECO:0000269|PubMed:24619089,
CC ECO:0000269|PubMed:24914988, ECO:0000305|PubMed:14559180}.
CC -!- MASS SPECTROMETRY: Mass=88426; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:27686148};
CC -!- DISRUPTION PHENOTYPE: Deletion is lethal. Depletion results in the
CC accumulation of incorrectly assembled outer membrane proteins,
CC including TolC, OmpF, OmpC and OmpA (PubMed:15851030, PubMed:16102012).
CC Decreased expression leads to decreased susceptibility to contact-
CC dependent growth inhibition (CDI), and decreased expression of outer
CC membrane proteins (including in this study LamB) as well as up-
CC regulation of periplasmic protease DegP (PubMed:18761695,
CC PubMed:23469034). {ECO:0000269|PubMed:15851030,
CC ECO:0000269|PubMed:16102012, ECO:0000269|PubMed:18761695,
CC ECO:0000269|PubMed:23469034}.
CC -!- SIMILARITY: Belongs to the BamA family. {ECO:0000255|HAMAP-
CC Rule:MF_01430}.
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DR EMBL; AF407013; AAL01379.1; -; Genomic_DNA.
DR EMBL; AY035865; AAK64508.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08606.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73288.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77852.2; -; Genomic_DNA.
DR PIR; A64742; A64742.
DR RefSeq; NP_414719.1; NC_000913.3.
DR RefSeq; WP_001240896.1; NZ_STEB01000032.1.
DR PDB; 2QCZ; X-ray; 2.70 A; A/B=21-351.
DR PDB; 2QDF; X-ray; 2.20 A; A=21-351.
DR PDB; 2V9H; NMR; -; A=21-184.
DR PDB; 3EFC; X-ray; 3.30 A; A=21-410.
DR PDB; 3OG5; X-ray; 2.69 A; A/B=264-424.
DR PDB; 3Q6B; X-ray; 1.50 A; A=266-420.
DR PDB; 4C4V; X-ray; 3.00 A; A=347-810, B=344-810.
DR PDB; 4N75; X-ray; 2.60 A; A/B=427-810.
DR PDB; 4PK1; X-ray; 3.10 A; A=175-424.
DR PDB; 4XGA; X-ray; 2.15 A; B=175-420.
DR PDB; 5AYW; X-ray; 3.56 A; A=22-810.
DR PDB; 5D0O; X-ray; 2.90 A; A=1-810.
DR PDB; 5D0Q; X-ray; 3.50 A; A/F=1-810.
DR PDB; 5EKQ; X-ray; 3.39 A; A=21-810.
DR PDB; 5LJO; EM; 4.90 A; A=24-806.
DR PDB; 6LYQ; X-ray; 3.19 A; A=1-810.
DR PDB; 6LYR; X-ray; 3.28 A; A=1-810.
DR PDB; 6LYS; X-ray; 3.05 A; A=1-810.
DR PDB; 6LYU; EM; 4.20 A; A=1-810.
DR PDB; 6SMX; EM; 6.65 A; A=24-806.
DR PDB; 6SN0; EM; 10.80 A; A=24-806.
DR PDB; 6SN2; EM; 9.50 A; A=24-806.
DR PDB; 6SN3; EM; 8.40 A; A=24-806.
DR PDB; 6SN4; EM; 9.50 A; A=24-806.
DR PDB; 6SN5; EM; 9.80 A; A=24-806.
DR PDB; 6SN7; EM; 8.90 A; A=24-806.
DR PDB; 6SN8; EM; 8.40 A; A=24-806.
DR PDB; 6SN9; EM; 9.80 A; A=24-806.
DR PDB; 6SO7; EM; 10.50 A; A=24-806.
DR PDB; 6SO8; EM; 9.80 A; A=24-806.
DR PDB; 6SOA; EM; 10.80 A; A=24-806.
DR PDB; 6SOB; EM; 8.50 A; A=24-806.
DR PDB; 6SOC; EM; 9.00 A; A=24-806.
DR PDB; 6SOG; EM; 8.30 A; A=24-806.
DR PDB; 6SOH; EM; 9.50 A; A=24-806.
DR PDB; 6SOJ; EM; 10.40 A; A=24-806.
DR PDB; 6T1W; X-ray; 3.79 A; A/B=1-810.
DR PDB; 6V05; EM; 4.10 A; A=1-810, F=1-810.
DR PDB; 7BNQ; EM; 4.10 A; A=1-810.
DR PDB; 7NBX; EM; 4.80 A; A=1-810.
DR PDB; 7NCS; EM; 7.10 A; A=1-810.
DR PDB; 7ND0; EM; 5.20 A; A=1-810.
DR PDB; 7NRI; EM; 3.03 A; A=21-808.
DR PDB; 7RI4; EM; 3.40 A; A=1-810.
DR PDB; 7RI5; EM; 4.00 A; A=1-810.
DR PDB; 7RI6; EM; 5.90 A; A=1-810.
DR PDB; 7RI7; EM; 8.00 A; A=1-810.
DR PDB; 7RI8; EM; 7.50 A; A=1-810.
DR PDB; 7RI9; EM; 6.90 A; A=1-810.
DR PDB; 7RJ5; EM; 7.00 A; A=1-810.
DR PDBsum; 2QCZ; -.
DR PDBsum; 2QDF; -.
DR PDBsum; 2V9H; -.
DR PDBsum; 3EFC; -.
DR PDBsum; 3OG5; -.
DR PDBsum; 3Q6B; -.
DR PDBsum; 4C4V; -.
DR PDBsum; 4N75; -.
DR PDBsum; 4PK1; -.
DR PDBsum; 4XGA; -.
DR PDBsum; 5AYW; -.
DR PDBsum; 5D0O; -.
DR PDBsum; 5D0Q; -.
DR PDBsum; 5EKQ; -.
DR PDBsum; 5LJO; -.
DR PDBsum; 6LYQ; -.
DR PDBsum; 6LYR; -.
DR PDBsum; 6LYS; -.
DR PDBsum; 6LYU; -.
DR PDBsum; 6SMX; -.
DR PDBsum; 6SN0; -.
DR PDBsum; 6SN2; -.
DR PDBsum; 6SN3; -.
DR PDBsum; 6SN4; -.
DR PDBsum; 6SN5; -.
DR PDBsum; 6SN7; -.
DR PDBsum; 6SN8; -.
DR PDBsum; 6SN9; -.
DR PDBsum; 6SO7; -.
DR PDBsum; 6SO8; -.
DR PDBsum; 6SOA; -.
DR PDBsum; 6SOB; -.
DR PDBsum; 6SOC; -.
DR PDBsum; 6SOG; -.
DR PDBsum; 6SOH; -.
DR PDBsum; 6SOJ; -.
DR PDBsum; 6T1W; -.
DR PDBsum; 6V05; -.
DR PDBsum; 7BNQ; -.
DR PDBsum; 7NBX; -.
DR PDBsum; 7NCS; -.
DR PDBsum; 7ND0; -.
DR PDBsum; 7NRI; -.
DR PDBsum; 7RI4; -.
DR PDBsum; 7RI5; -.
DR PDBsum; 7RI6; -.
DR PDBsum; 7RI7; -.
DR PDBsum; 7RI8; -.
DR PDBsum; 7RI9; -.
DR PDBsum; 7RJ5; -.
DR AlphaFoldDB; P0A940; -.
DR SMR; P0A940; -.
DR BioGRID; 4259504; 747.
DR ComplexPortal; CPX-1923; BAM complex.
DR DIP; DIP-36019N; -.
DR IntAct; P0A940; 14.
DR STRING; 511145.b0177; -.
DR CarbonylDB; P0A940; -.
DR SWISS-2DPAGE; P0A940; -.
DR jPOST; P0A940; -.
DR PaxDb; P0A940; -.
DR PRIDE; P0A940; -.
DR EnsemblBacteria; AAC73288; AAC73288; b0177.
DR EnsemblBacteria; BAA77852; BAA77852; BAA77852.
DR GeneID; 66671535; -.
DR GeneID; 944870; -.
DR KEGG; ecj:JW0172; -.
DR KEGG; eco:b0177; -.
DR PATRIC; fig|1411691.4.peg.2102; -.
DR EchoBASE; EB2541; -.
DR eggNOG; COG4775; Bacteria.
DR HOGENOM; CLU_007664_1_0_6; -.
DR InParanoid; P0A940; -.
DR OMA; IFMPAFG; -.
DR PhylomeDB; P0A940; -.
DR BioCyc; EcoCyc:G6093-MON; -.
DR EvolutionaryTrace; P0A940; -.
DR PRO; PR:P0A940; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990063; C:Bam protein complex; IDA:EcoCyc.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IDA:ComplexPortal.
DR GO; GO:0051205; P:protein insertion into membrane; IDA:ComplexPortal.
DR HAMAP; MF_01430; OM_assembly_BamA; 1.
DR InterPro; IPR000184; Bac_surfAg_D15.
DR InterPro; IPR010827; BamA/TamA_POTRA.
DR InterPro; IPR039910; D15-like.
DR InterPro; IPR023707; OM_assembly_BamA.
DR InterPro; IPR034746; POTRA.
DR PANTHER; PTHR12815; PTHR12815; 1.
DR PANTHER; PTHR12815:SF23; PTHR12815:SF23; 1.
DR Pfam; PF01103; Omp85; 1.
DR Pfam; PF07244; POTRA; 4.
DR PIRSF; PIRSF006076; OM_assembly_OMP85; 1.
DR TIGRFAMs; TIGR03303; OM_YaeT; 1.
DR PROSITE; PS51779; POTRA; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell outer membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01430,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 21..810
FT /note="Outer membrane protein assembly factor BamA"
FT /id="PRO_0000033470"
FT TOPO_DOM 21..424
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 425..433
FT /note="Beta stranded; Name=Strand 1"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 434..435
FT /note="Extracellular; loop 1"
FT /evidence="ECO:0000305"
FT TRANSMEM 436..446
FT /note="Beta stranded; Name=Strand 2"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 447..454
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 455..462
FT /note="Beta stranded; Name=Strand 3"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 463..465
FT /note="Extracellular; loop 2"
FT /evidence="ECO:0000305"
FT TRANSMEM 466..475
FT /note="Beta stranded; Name=Strand 4"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 476..483
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 484..495
FT /note="Beta stranded; Name=Strand 5"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 496..504
FT /note="Extracellular; loop 3"
FT /evidence="ECO:0000305"
FT TRANSMEM 505..506
FT /note="Beta stranded; Name=Strand 6"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 507..522
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 523..535
FT /note="Beta stranded; Name=Strand 7"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 536..563
FT /note="Extracellular; loop 4"
FT /evidence="ECO:0000269|PubMed:23882017,
FT ECO:0000269|PubMed:24914988"
FT TRANSMEM 564..577
FT /note="Beta stranded; Name=Strand 8"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 578..590
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 591..600
FT /note="Beta stranded; Name=Strand 9"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 601..608
FT /note="Extracellular; loop 5"
FT /evidence="ECO:0000305"
FT TRANSMEM 609..619
FT /note="Beta stranded; Name=Strand 10"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 620..628
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 629..639
FT /note="Beta stranded; Name=Strand 11"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 640..708
FT /note="Extracellular; loop 6"
FT /evidence="ECO:0000269|PubMed:23882017,
FT ECO:0000269|PubMed:24914988"
FT TRANSMEM 709..718
FT /note="Beta stranded; Name=Strand 12"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 719..732
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 733..745
FT /note="Beta stranded; Name=Strand 13"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 746..767
FT /note="Extracellular; loop 7"
FT /evidence="ECO:0000305"
FT TRANSMEM 768..777
FT /note="Beta stranded; Name=Strand 14"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 778
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 779..789
FT /note="Beta stranded; Name=Strand 15"
FT /evidence="ECO:0000269|PubMed:24914988"
FT TOPO_DOM 790..803
FT /note="Extracellular; loop 8"
FT /evidence="ECO:0000305"
FT TRANSMEM 804..808
FT /note="Beta stranded; Name=Strand 16"
FT /evidence="ECO:0000269|PubMed:24914988"
FT DOMAIN 24..91
FT /note="POTRA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115,
FT ECO:0000305|PubMed:14559180"
FT DOMAIN 92..172
FT /note="POTRA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115,
FT ECO:0000305|PubMed:14559180"
FT DOMAIN 175..263
FT /note="POTRA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115,
FT ECO:0000305|PubMed:14559180"
FT DOMAIN 266..344
FT /note="POTRA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115,
FT ECO:0000305|PubMed:14559180"
FT DOMAIN 347..421
FT /note="POTRA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115,
FT ECO:0000305|PubMed:14559180"
FT MUTAGEN 181
FT /note="N->A: Lethal, protein does not accumulate."
FT /evidence="ECO:0000269|PubMed:26900875"
FT MUTAGEN 251
FT /note="K->A: Lethal, protein does not accumulate."
FT /evidence="ECO:0000269|PubMed:26900875"
FT MUTAGEN 259
FT /note="N->A: Lethal, protein does not accumulate."
FT /evidence="ECO:0000269|PubMed:26900875"
FT MUTAGEN 351..353
FT /note="KIR->PIP: Lethal, wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 351
FT /note="K->P: Reduces cell growth, wild-type protein
FT levels."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 366
FT /note="R->E: Severely impairs cell growth, wild-type
FT protein levels."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 373
FT /note="E->K: Lethal, wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:26900875,
FT ECO:0000269|PubMed:26901871"
FT MUTAGEN 393
FT /note="G->C: No effect. Lethal; when associated with C-584,
FT probably locks protein in a single conformation that
FT prevents movement, growth restored by strong reducing
FT agent."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 415..419
FT /note="VYKVK->PYKVP: Lethal, wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 415..417
FT /note="VYK->PYP: Lethal, wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 417..419
FT /note="KVK->PVP: Lethal, wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 429
FT /note="G->P: Lethal, wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:26900875"
FT MUTAGEN 430
FT /note="I->C: Reduced folding of OmpT; when associated with
FT C-808, traps protein in lateral closed conformation, growth
FT restored by reducing agent."
FT /evidence="ECO:0000269|PubMed:27686148"
FT MUTAGEN 435
FT /note="E->C: No effect. Lethal; when associated with C-658
FT or C-665, probably locks protein in a single conformation
FT that prevents movement, growth restored by strong reducing
FT agent."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 435
FT /note="E->L: Very minor growth defect. Lethal; when
FT associated with L-800."
FT /evidence="ECO:0000269|PubMed:24619089"
FT MUTAGEN 464
FT /note="D->L: Very minor growth defect."
FT /evidence="ECO:0000269|PubMed:24619089"
FT MUTAGEN 500
FT /note="D->L: Very minor growth defect."
FT /evidence="ECO:0000269|PubMed:24619089"
FT MUTAGEN 547
FT /note="R->A: Lethal."
FT /evidence="ECO:0000269|PubMed:24619089"
FT MUTAGEN 554..562
FT /note="EHPSTSDQD->VDYPYDVPDYA: Loop 4 to HA epitope; still
FT susceptible to CdiA-EC93."
FT /evidence="ECO:0000269|PubMed:23882017"
FT MUTAGEN 556..563
FT /note="PSTSDQDN->G: Delta loop 4; slight increase in
FT resistance to CdiA-EC93, forms aggregates with CdiA-EC93
FT cells."
FT /evidence="ECO:0000269|PubMed:23882017"
FT MUTAGEN 584
FT /note="G->C: No effect. Lethal; when associated with C-393,
FT probably locks protein in a single conformation that
FT prevents movement, growth restored by strong reducing
FT agent."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 658
FT /note="S->C: No effect. Lethal; when associated with C-435,
FT probably locks protein in a single conformation that
FT prevents movement, growth restored by strong reducing
FT agent."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 661
FT /note="R->A: Slow growth on solid and liquid media, less
FT protein accumulates which is more proteinase sensitive."
FT /evidence="ECO:0000269|PubMed:24619089"
FT MUTAGEN 665
FT /note="S->C: No effect. Lethal; when associated with C-435,
FT probably locks protein in a single conformation that
FT prevents movement, growth restored by strong reducing
FT agent."
FT /evidence="ECO:0000269|PubMed:26901871"
FT MUTAGEN 673..702
FT /note="Missing: Lethal."
FT /evidence="ECO:0000269|PubMed:24619089"
FT MUTAGEN 675..701
FT /note="FPHQASNYDPDYDYECATQDGAKDLCK->G: Delta loop 6; fully
FT resistant to CdiA-EC93, does not form aggregates with CdiA-
FT EC93 cells."
FT /evidence="ECO:0000269|PubMed:23882017"
FT MUTAGEN 677..685
FT /note="HQASNYDPD->VDYPYDVPDYA: Loop 6 to HA epitope; still
FT susceptible to CdiA-EC93."
FT /evidence="ECO:0000269|PubMed:23882017"
FT MUTAGEN 740
FT /note="D->A: Slow growth on solid and liquid media, less
FT protein accumulates which is more proteinase sensitive."
FT /evidence="ECO:0000269|PubMed:24619089"
FT MUTAGEN 754..755
FT /note="YS->VDYPYDVPDYA: Loop 7 to HA epitope; fully
FT resistant to CdiA-EC93, does not form aggregates with CdiA-
FT EC93 cells."
FT /evidence="ECO:0000269|PubMed:23882017"
FT MUTAGEN 800
FT /note="E->L: Very minor growth defect. Lethal; when
FT associated with L-435."
FT /evidence="ECO:0000269|PubMed:24619089"
FT MUTAGEN 808
FT /note="K->C: Reduced folding of OmpT; when associated with
FT C-430, traps protein in lateral closed conformation, growth
FT restored by reducing agent."
FT /evidence="ECO:0000269|PubMed:27686148"
FT CONFLICT 115
FT /note="E -> Q (in Ref. 2; AAK64508)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="S -> I (in Ref. 2; AAK64508)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="K -> R (in Ref. 2; AAK64508)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="R -> C (in Ref. 2; AAK64508)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="A -> T (in Ref. 2; AAK64508)"
FT /evidence="ECO:0000305"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2QDF"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2QDF"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:2QDF"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:2QDF"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6LYS"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:2QDF"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:2QDF"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:2QDF"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2QCZ"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:2QDF"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2QDF"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3EFC"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6LYQ"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:2QDF"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:2QDF"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2QDF"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:2QDF"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2QDF"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:2QDF"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:4XGA"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2QCZ"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:4XGA"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2QDF"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:6LYQ"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:3EFC"
FT HELIX 216..231
FT /evidence="ECO:0007829|PDB:4XGA"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:4XGA"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:4XGA"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:4XGA"
FT STRAND 267..276
FT /evidence="ECO:0007829|PDB:3Q6B"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:5D0O"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:3Q6B"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:7NRI"
FT HELIX 298..313
FT /evidence="ECO:0007829|PDB:3Q6B"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:3Q6B"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:4XGA"
FT STRAND 321..329
FT /evidence="ECO:0007829|PDB:3Q6B"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:3Q6B"
FT STRAND 334..342
FT /evidence="ECO:0007829|PDB:3Q6B"
FT STRAND 348..356
FT /evidence="ECO:0007829|PDB:3Q6B"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:3Q6B"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:3Q6B"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:4C4V"
FT HELIX 379..392
FT /evidence="ECO:0007829|PDB:3Q6B"
FT STRAND 396..405
FT /evidence="ECO:0007829|PDB:3Q6B"
FT STRAND 408..419
FT /evidence="ECO:0007829|PDB:3Q6B"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:4N75"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 437..453
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 464..475
FT /evidence="ECO:0007829|PDB:4N75"
FT TURN 479..482
FT /evidence="ECO:0007829|PDB:4C4V"
FT STRAND 484..495
FT /evidence="ECO:0007829|PDB:4N75"
FT HELIX 496..499
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 505..520
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 523..537
FT /evidence="ECO:0007829|PDB:4N75"
FT HELIX 543..551
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:6LYS"
FT STRAND 564..579
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 589..600
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:5D0O"
FT STRAND 608..620
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:4C4V"
FT STRAND 627..643
FT /evidence="ECO:0007829|PDB:4N75"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:7NRI"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:5D0O"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:5D0O"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:5D0O"
FT STRAND 700..705
FT /evidence="ECO:0007829|PDB:5D0O"
FT STRAND 708..720
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:5D0O"
FT TURN 727..731
FT /evidence="ECO:0007829|PDB:5D0O"
FT STRAND 733..745
FT /evidence="ECO:0007829|PDB:4N75"
FT TURN 751..756
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 767..778
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 781..792
FT /evidence="ECO:0007829|PDB:4N75"
FT STRAND 802..809
FT /evidence="ECO:0007829|PDB:4N75"
SQ 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
