BAMB_ECOLI
ID BAMB_ECOLI Reviewed; 392 AA.
AC P77774;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Outer membrane protein assembly factor BamB {ECO:0000255|HAMAP-Rule:MF_00923};
DE Flags: Precursor;
GN Name=bamB {ECO:0000255|HAMAP-Rule:MF_00923}; Synonyms=yfgL;
GN OrderedLocusNames=b2512, JW2496;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
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 [5]
RP SUBUNIT, AND INTERACTION WITH BAMA.
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 [6]
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 [7]
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 [8] {ECO:0007744|PDB:3PRW}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 21-392.
RX PubMed=21236263; DOI=10.1016/j.jmb.2011.01.002;
RA Heuck A., Schleiffer A., Clausen T.;
RT "Augmenting beta-augmentation: structural basis of how BamB binds BamA and
RT may support folding of outer membrane proteins.";
RL J. Mol. Biol. 406:659-666(2011).
RN [9] {ECO:0007744|PDB:2YH3}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 22-392, INTERACTION WITH BAMA,
RP SUBUNIT, AND FUNCTION.
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 [10] {ECO:0007744|PDB:3P1L}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 21-392.
RX PubMed=21168416; DOI=10.1016/j.jmb.2010.12.020;
RA Kim K.H., Paetzel M.;
RT "Crystal structure of Escherichia coli BamB, a lipoprotein component of the
RT beta-barrel assembly machinery complex.";
RL J. Mol. Biol. 406:667-678(2011).
RN [11] {ECO:0007744|PDB:3Q7M, ECO:0007744|PDB:3Q7N, ECO:0007744|PDB:3Q7O}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 21-392, FUNCTION, AND SUBUNIT.
RX PubMed=21277859; DOI=10.1016/j.jmb.2011.01.042;
RA Noinaj N., Fairman J.W., Buchanan S.K.;
RT "The crystal structure of BamB suggests interactions with BamA and its role
RT within the BAM complex.";
RL J. Mol. Biol. 407:248-260(2011).
RN [12] {ECO:0007744|PDB:5LJO}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 22-392 IN LATERAL OPEN
RP BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY,
RP DIACYLGLYCEROL AT CYS-20, AND PALMITOYLATION AT CYS-20.
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 [13] {ECO:0007744|PDB:5AYW}
RP X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 20-392 IN LATERAL CLOSED BAM
RP COMPLEX, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [14] {ECO:0007744|PDB:5D0O}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX,
RP REACTION MECHANISM, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
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. Nonessential member of the complex, which may
CC orient the flexible periplasmic domain of BamA for interaction with
CC other Bam components, chaperones and nascent outer membrane proteins.
CC Efficient substrate folding and insertion into the outer membrane
CC requires all 5 subunits (PubMed:20378773, PubMed:21823654,
CC PubMed:27686148). A lateral gate may open between the first and last
CC strands of the BamA beta-barrel that allows substrate to insert into
CC the outer membrane; comparison of the structures of complete and nearly
CC complete Bam complexes show there is considerable movement of all 5
CC proteins (PubMed:27686148, PubMed:26900875, PubMed:26901871).
CC {ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21277859,
CC ECO:0000269|PubMed:21586578, ECO:0000269|PubMed:21823654,
CC ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871,
CC ECO:0000269|PubMed:27686148}.
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 Monomer. Interacts directly with BamA. The Bam complex has the shape of
CC a hat, with the BamA beta-barrel crown in the outer membrane and the
CC periplasmic brim formed by the BamA POTRA domains and the 4
CC lipoproteins (PubMed:27686148, PubMed:26900875, PubMed:26901871).
CC {ECO:0000269|PubMed:15851030, ECO:0000269|PubMed:16824102,
CC ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21277859,
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 P77774; P0A940: bamA; NbExp=23; IntAct=EBI-907297, EBI-907371;
CC P77774; P77774: bamB; NbExp=2; IntAct=EBI-907297, EBI-907297;
CC P77774; P0ABZ6: surA; NbExp=2; IntAct=EBI-907297, EBI-558651;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00923, ECO:0000269|PubMed:15851030,
CC ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_00923, ECO:0000269|PubMed:15851030,
CC ECO:0000269|PubMed:27686148}.
CC -!- MASS SPECTROMETRY: Mass=40643; Method=Electrospray; Note=With 3
CC palmitic acid (C16) acyl chains.;
CC Evidence={ECO:0000269|PubMed:27686148};
CC -!- MASS SPECTROMETRY: Mass=40663; Method=Electrospray; Note=With 2
CC palmitic (C16) and 1 stearic (C18) acid acyl chains.;
CC Evidence={ECO:0000269|PubMed:27686148};
CC -!- SIMILARITY: Belongs to the BamB family. {ECO:0000255|HAMAP-
CC Rule:MF_00923}.
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DR EMBL; U00096; AAC75565.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16398.1; -; Genomic_DNA.
DR PIR; G65027; G65027.
DR RefSeq; NP_417007.1; NC_000913.3.
DR RefSeq; WP_001177052.1; NZ_LN832404.1.
DR PDB; 2YH3; X-ray; 2.60 A; A=22-392.
DR PDB; 2YMS; X-ray; 2.10 A; A=62-191, B=113-186, C=248-322, D=247-320.
DR PDB; 3P1L; X-ray; 2.60 A; A=21-392.
DR PDB; 3PRW; X-ray; 1.80 A; A=21-392.
DR PDB; 3Q7M; X-ray; 1.65 A; A=21-392.
DR PDB; 3Q7N; X-ray; 1.77 A; A=21-392.
DR PDB; 3Q7O; X-ray; 2.09 A; A=21-392.
DR PDB; 4PK1; X-ray; 3.10 A; A=21-392.
DR PDB; 4XGA; X-ray; 2.15 A; A=20-392.
DR PDB; 5AYW; X-ray; 3.56 A; B=20-392.
DR PDB; 5D0O; X-ray; 2.90 A; B=1-392.
DR PDB; 5LJO; EM; 4.90 A; B=22-392.
DR PDB; 6LYQ; X-ray; 3.19 A; B=1-392.
DR PDB; 6LYR; X-ray; 3.28 A; B=1-392.
DR PDB; 6LYS; X-ray; 3.05 A; B=1-392.
DR PDB; 6LYU; EM; 4.20 A; B=1-392.
DR PDB; 6SMX; EM; 6.65 A; B=22-392.
DR PDB; 6SN0; EM; 10.80 A; B=22-392.
DR PDB; 6SN2; EM; 9.50 A; B=22-392.
DR PDB; 6SN3; EM; 8.40 A; B=22-392.
DR PDB; 6SN4; EM; 9.50 A; B=22-392.
DR PDB; 6SN5; EM; 9.80 A; B=22-392.
DR PDB; 6SN7; EM; 8.90 A; B=22-392.
DR PDB; 6SN8; EM; 8.40 A; B=22-392.
DR PDB; 6SN9; EM; 9.80 A; B=22-392.
DR PDB; 6SO7; EM; 10.50 A; B=22-392.
DR PDB; 6SO8; EM; 9.80 A; B=22-392.
DR PDB; 6SOA; EM; 10.80 A; B=22-392.
DR PDB; 6SOB; EM; 8.50 A; B=22-392.
DR PDB; 6SOC; EM; 9.00 A; B=22-392.
DR PDB; 6SOG; EM; 8.30 A; B=22-392.
DR PDB; 6SOH; EM; 9.50 A; B=22-392.
DR PDB; 6SOJ; EM; 10.40 A; B=22-392.
DR PDB; 6V05; EM; 4.10 A; B=1-392.
DR PDB; 7BNQ; EM; 4.10 A; B=1-392.
DR PDB; 7NBX; EM; 4.80 A; B=1-392.
DR PDB; 7NCS; EM; 7.10 A; B=1-392.
DR PDB; 7ND0; EM; 5.20 A; B=1-392.
DR PDB; 7NRI; EM; 3.03 A; B=20-392.
DR PDB; 7TTC; EM; 3.60 A; B=20-392.
DR PDBsum; 2YH3; -.
DR PDBsum; 2YMS; -.
DR PDBsum; 3P1L; -.
DR PDBsum; 3PRW; -.
DR PDBsum; 3Q7M; -.
DR PDBsum; 3Q7N; -.
DR PDBsum; 3Q7O; -.
DR PDBsum; 4PK1; -.
DR PDBsum; 4XGA; -.
DR PDBsum; 5AYW; -.
DR PDBsum; 5D0O; -.
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; 6V05; -.
DR PDBsum; 7BNQ; -.
DR PDBsum; 7NBX; -.
DR PDBsum; 7NCS; -.
DR PDBsum; 7ND0; -.
DR PDBsum; 7NRI; -.
DR PDBsum; 7TTC; -.
DR AlphaFoldDB; P77774; -.
DR SMR; P77774; -.
DR BioGRID; 4260587; 321.
DR ComplexPortal; CPX-1923; BAM complex.
DR DIP; DIP-12042N; -.
DR IntAct; P77774; 9.
DR STRING; 511145.b2512; -.
DR TCDB; 1.B.33.1.3; the outer membrane protein insertion porin (bam complex) (ompip) family.
DR jPOST; P77774; -.
DR PaxDb; P77774; -.
DR PRIDE; P77774; -.
DR EnsemblBacteria; AAC75565; AAC75565; b2512.
DR EnsemblBacteria; BAA16398; BAA16398; BAA16398.
DR GeneID; 946982; -.
DR KEGG; ecj:JW2496; -.
DR KEGG; eco:b2512; -.
DR PATRIC; fig|1411691.4.peg.4224; -.
DR EchoBASE; EB3960; -.
DR eggNOG; COG1520; Bacteria.
DR HOGENOM; CLU_027480_0_1_6; -.
DR InParanoid; P77774; -.
DR OMA; GRVLWQR; -.
DR PhylomeDB; P77774; -.
DR BioCyc; EcoCyc:G7320-MON; -.
DR EvolutionaryTrace; P77774; -.
DR PRO; PR:P77774; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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; 2.130.10.10; -; 1.
DR HAMAP; MF_00923; OM_assembly_BamB; 1.
DR InterPro; IPR017687; BamB.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 7.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03300; assembly_YfgL; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00923"
FT CHAIN 20..392
FT /note="Outer membrane protein assembly factor BamB"
FT /id="PRO_0000042211"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:27686148"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:27686148"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:3Q7O"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 53..58
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3Q7N"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:4XGA"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6LYQ"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:6LYQ"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:3Q7M"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:3Q7M"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:2YH3"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:3Q7M"
SQ SEQUENCE 392 AA; 41887 MW; BCFAFA061A486B31 CRC64;
MQLRKLLLPG LLSVTLLSGC SLFNSEEDVV KMSPLPTVEN QFTPTTAWST SVGSGIGNFY
SNLHPALADN VVYAADRAGL VKALNADDGK EIWSVSLAEK DGWFSKEPAL LSGGVTVSGG
HVYIGSEKAQ VYALNTSDGT VAWQTKVAGE ALSRPVVSDG LVLIHTSNGQ LQALNEADGA
VKWTVNLDMP SLSLRGESAP TTAFGAAVVG GDNGRVSAVL MEQGQMIWQQ RISQATGSTE
IDRLSDVDTT PVVVNGVVFA LAYNGNLTAL DLRSGQIMWK RELGSVNDFI VDGNRIYLVD
QNDRVMALTI DGGVTLWTQS DLLHRLLTSP VLYNGNLVVG DSEGYLHWIN VEDGRFVAQQ
KVDSSGFQTE PVAADGKLLI QAKDGTVYSI TR
