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 27-MAR-2024, entry version 153. 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}; GN Synonyms=yaeT, yzzN, yzzY; OrderedLocusNames=b0177, JW0172; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 6FSU; X-ray; 2.60 A; A/B=421-810. 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; 6QGW; X-ray; 1.94 A; A=421-810. DR PDB; 6QGX; X-ray; 2.20 A; A=421-810. DR PDB; 6QGY; X-ray; 2.51 A; A/C=421-810. 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; 7NRE; X-ray; 2.30 A; A=421-810. DR PDB; 7NRF; X-ray; 2.20 A; A=421-810. DR PDB; 7NRI; EM; 3.03 A; A=21-808. DR PDB; 7P1C; X-ray; 2.50 A; A=421-810. DR PDB; 7R1V; X-ray; 2.50 A; A=421-810. DR PDB; 7R1W; EM; 3.60 A; A=1-809. 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 PDB; 7TSZ; EM; 4.50 A; A=22-810. DR PDB; 7TT0; EM; 4.30 A; A=22-810. DR PDB; 7TT1; EM; 4.30 A; A=22-810. DR PDB; 7TT2; EM; 4.20 A; A=22-810. DR PDB; 7TT3; EM; 4.30 A; A=22-810. DR PDB; 7TT4; EM; 4.20 A; A=22-810. DR PDB; 7TT5; EM; 4.30 A; A=22-810. DR PDB; 7TT6; EM; 4.30 A; A=22-810. DR PDB; 7TT7; EM; 4.80 A; A=22-810. DR PDB; 7TTC; EM; 3.60 A; A=22-810. DR PDB; 7YE4; EM; 3.40 A; A=1-810. DR PDB; 7YE6; EM; 3.40 A; A=1-810. DR PDB; 8ADG; EM; 3.00 A; A=1-810. DR PDB; 8ADI; EM; 3.40 A; A=1-810. DR PDB; 8BNZ; EM; 3.50 A; A=1-810. DR PDB; 8BO2; EM; 3.10 A; A=24-810. DR PDB; 8BVQ; EM; 3.30 A; A=21-810. 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; 6FSU; -. DR PDBsum; 6LYQ; -. DR PDBsum; 6LYR; -. DR PDBsum; 6LYS; -. DR PDBsum; 6LYU; -. DR PDBsum; 6QGW; -. DR PDBsum; 6QGX; -. DR PDBsum; 6QGY; -. 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; 7NRE; -. DR PDBsum; 7NRF; -. DR PDBsum; 7NRI; -. DR PDBsum; 7P1C; -. DR PDBsum; 7R1V; -. DR PDBsum; 7R1W; -. DR PDBsum; 7RI4; -. DR PDBsum; 7RI5; -. DR PDBsum; 7RI6; -. DR PDBsum; 7RI7; -. DR PDBsum; 7RI8; -. DR PDBsum; 7RI9; -. DR PDBsum; 7RJ5; -. DR PDBsum; 7TSZ; -. DR PDBsum; 7TT0; -. DR PDBsum; 7TT1; -. DR PDBsum; 7TT2; -. DR PDBsum; 7TT3; -. DR PDBsum; 7TT4; -. DR PDBsum; 7TT5; -. DR PDBsum; 7TT6; -. DR PDBsum; 7TT7; -. DR PDBsum; 7TTC; -. DR PDBsum; 7YE4; -. DR PDBsum; 7YE6; -. DR PDBsum; 8ADG; -. DR PDBsum; 8ADI; -. DR PDBsum; 8BNZ; -. DR PDBsum; 8BO2; -. DR PDBsum; 8BVQ; -. DR AlphaFoldDB; P0A940; -. DR EMDB; EMD-10247; -. DR EMDB; EMD-10248; -. DR EMDB; EMD-10249; -. DR EMDB; EMD-10250; -. DR EMDB; EMD-10251; -. DR EMDB; EMD-10252; -. DR EMDB; EMD-10253; -. DR EMDB; EMD-10254; -. DR EMDB; EMD-10255; -. DR EMDB; EMD-10268; -. DR EMDB; EMD-10269; -. DR EMDB; EMD-10270; -. DR EMDB; EMD-10271; -. DR EMDB; EMD-10272; -. DR EMDB; EMD-10274; -. DR EMDB; EMD-10275; -. DR EMDB; EMD-10276; -. DR EMDB; EMD-12232; -. DR EMDB; EMD-12262; -. DR EMDB; EMD-12263; -. DR EMDB; EMD-12271; -. DR EMDB; EMD-12272; -. DR EMDB; EMD-12546; -. DR EMDB; EMD-16137; -. DR EMDB; EMD-16138; -. DR EMDB; EMD-16268; -. DR EMDB; EMD-20969; -. DR EMDB; EMD-24473; -. DR EMDB; EMD-24474; -. DR EMDB; EMD-24475; -. DR EMDB; EMD-24476; -. DR EMDB; EMD-24477; -. DR EMDB; EMD-24478; -. DR EMDB; EMD-24481; -. DR EMDB; EMD-26105; -. DR EMDB; EMD-26106; -. DR EMDB; EMD-26107; -. DR EMDB; EMD-26108; -. DR EMDB; EMD-26109; -. DR EMDB; EMD-26110; -. DR EMDB; EMD-26111; -. DR EMDB; EMD-26112; -. DR EMDB; EMD-26113; -. DR EMDB; EMD-30018; -. DR EMDB; EMD-33763; -. DR EMDB; EMD-33765; -. DR EMDB; EMD-4061; -. 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 jPOST; P0A940; -. DR PaxDb; 511145-b0177; -. DR EnsemblBacteria; AAC73288; AAC73288; b0177. DR GeneID; 75202010; -. 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; TNPRIFD; -. DR OrthoDB; 9803054at2; -. DR PhylomeDB; P0A940; -. DR BioCyc; EcoCyc:G6093-MONOMER; -. 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: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 Gene3D; 3.10.20.310; membrane protein fhac; 5. DR Gene3D; 2.40.160.50; membrane protein fhac: a member of the omp85/tpsb transporter family; 1. 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 NCBIfam; TIGR03303; OM_YaeT; 1. DR PANTHER; PTHR12815:SF23; OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAMA; 1. DR PANTHER; PTHR12815; SORTING AND ASSEMBLY MACHINERY SAMM50 PROTEIN FAMILY MEMBER; 1. DR Pfam; PF01103; Omp85; 1. DR Pfam; PF07244; POTRA; 4. DR PIRSF; PIRSF006076; OM_assembly_OMP85; 1. DR PROSITE; PS51779; POTRA; 5. DR SWISS-2DPAGE; P0A940; -. 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 FT CdiA-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 FT CdiA-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 STRAND 50..53 FT /evidence="ECO:0007829|PDB:8ADG" 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:6QGW" FT TURN 434..436 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 437..446 FT /evidence="ECO:0007829|PDB:6QGW" FT HELIX 449..451 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 455..462 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 464..475 FT /evidence="ECO:0007829|PDB:6QGW" FT HELIX 476..478 FT /evidence="ECO:0007829|PDB:6QGY" FT TURN 479..482 FT /evidence="ECO:0007829|PDB:4C4V" FT STRAND 484..495 FT /evidence="ECO:0007829|PDB:6QGW" FT HELIX 496..499 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 501..503 FT /evidence="ECO:0007829|PDB:7P1C" FT STRAND 505..520 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 523..537 FT /evidence="ECO:0007829|PDB:6QGW" FT HELIX 543..551 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 558..560 FT /evidence="ECO:0007829|PDB:6LYS" FT STRAND 564..579 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 584..586 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 589..600 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 604..606 FT /evidence="ECO:0007829|PDB:7NRF" FT STRAND 608..622 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 627..641 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 642..644 FT /evidence="ECO:0007829|PDB:4C4V" FT HELIX 648..650 FT /evidence="ECO:0007829|PDB:6QGW" FT TURN 657..659 FT /evidence="ECO:0007829|PDB:8ADG" FT STRAND 671..674 FT /evidence="ECO:0007829|PDB:6QGW" 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:6QGW" FT STRAND 708..720 FT /evidence="ECO:0007829|PDB:6QGW" FT TURN 723..725 FT /evidence="ECO:0007829|PDB:6QGX" FT TURN 727..729 FT /evidence="ECO:0007829|PDB:6QGW" FT HELIX 730..732 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 733..745 FT /evidence="ECO:0007829|PDB:6QGW" FT HELIX 751..753 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 755..757 FT /evidence="ECO:0007829|PDB:5EKQ" FT STRAND 767..778 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 781..792 FT /evidence="ECO:0007829|PDB:6QGW" FT STRAND 802..806 FT /evidence="ECO:0007829|PDB:6QGW" 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 //