BAMC_ECOLI
ID BAMC_ECOLI Reviewed; 344 AA.
AC P0A903; P21167; P76564;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Outer membrane protein assembly factor BamC {ECO:0000255|HAMAP-Rule:MF_00924};
DE Flags: Precursor;
GN Name=bamC {ECO:0000255|HAMAP-Rule:MF_00924}; Synonyms=dapX, nlpB;
GN OrderedLocusNames=b2477, JW2462;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL AT CYS-25, AND
RP PALMITOYLATION AT CYS-25.
RC STRAIN=K12;
RX PubMed=1885529; DOI=10.1128/jb.173.17.5523-5531.1991;
RA Bouvier J., Pugsley A.P., Stragier P.;
RT "A gene for a new lipoprotein in the dapA-purC interval of the Escherichia
RT coli chromosome.";
RL J. Bacteriol. 173:5523-5531(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2120198; DOI=10.1128/jb.172.10.6035-6041.1990;
RA Tiedemann A.A., Demarini D.J., Parker J., Smith J.M.;
RT "DNA sequence of the purC gene encoding 5'-phosphoribosyl-5-aminoimidazole-
RT 4-N-succinocarboxamide synthetase and organization of the dapA-purC region
RT of Escherichia coli K-12.";
RL J. Bacteriol. 172:6035-6041(1990).
RN [3]
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 [4]
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 [5]
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 [6]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [7]
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 [8]
RP SUBUNIT, AND INTERACTION WITH 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 [9]
RP SECONDARY STRUCTURE.
RX PubMed=19888691; DOI=10.1007/s12104-009-9175-3;
RA Knowles T.J., McClelland D.M., Rajesh S., Henderson I.R., Overduin M.;
RT "Secondary structure and (1)H, (13)C and (15)N backbone resonance
RT assignments of BamC, a component of the outer membrane protein assembly
RT machinery in Escherichia coli.";
RL Biomol. NMR. Assign. 3:203-206(2009).
RN [10]
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 [11]
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 [12]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=22178970; DOI=10.1128/jb.06426-11;
RA Rigel N.W., Schwalm J., Ricci D.P., Silhavy T.J.;
RT "BamE modulates the Escherichia coli beta-barrel assembly machine component
RT BamA.";
RL J. Bacteriol. 194:1002-1008(2012).
RN [13]
RP CRYSTALLIZATION.
RX PubMed=21139201; DOI=10.1107/s1744309110034160;
RA Albrecht R., Zeth K.;
RT "Crystallization and preliminary X-ray data collection of the Escherichia
RT coli lipoproteins BamC, BamD and BamE.";
RL Acta Crystallogr. F 66:1586-1590(2010).
RN [14] {ECO:0007744|PDB:3SNS}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 224-343, AND DOMAIN.
RX PubMed=22102230; DOI=10.1107/s174430911103363x;
RA Kim K.H., Aulakh S., Tan W., Paetzel M.;
RT "Crystallographic analysis of the C-terminal domain of the Escherichia coli
RT lipoprotein BamC.";
RL Acta Crystallogr. F 67:1350-1358(2011).
RN [15] {ECO:0007744|PDB:2YH5, ECO:0007744|PDB:2YH6}
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 226-344.
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 [16] {ECO:0007744|PDB:3TGO}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 26-344, INTERACTION WITH BAMD,
RP AND DOMAIN.
RC STRAIN=K12;
RX PubMed=21937441; DOI=10.1074/jbc.m111.298166;
RA Kim K.H., Aulakh S., Paetzel M.;
RT "Crystal structure of beta-barrel assembly machinery BamCD protein
RT complex.";
RL J. Biol. Chem. 286:39116-39121(2011).
RN [17] {ECO:0007744|PDB:2LAE, ECO:0007744|PDB:2LAF}
RP STRUCTURE BY NMR OF 101-344, AND DOMAIN.
RX PubMed=21624375; DOI=10.1016/j.jmb.2011.05.022;
RA Warner L.R., Varga K., Lange O.F., Baker S.L., Baker D., Sousa M.C.,
RA Pardi A.;
RT "Structure of the BamC two-domain protein obtained by Rosetta with a
RT limited NMR data set.";
RL J. Mol. Biol. 411:83-95(2011).
RN [18] {ECO:0007744|PDB:5LJO}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 25-189 IN LATERAL OPEN
RP BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, AND
RP LIPIDATION.
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 [19] {ECO:0007744|PDB:5AYW}
RP X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 33-88 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 [20] {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, 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).
RN [21] {ECO:0007744|PDB:5EKQ}
RP X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 25-344 OF LATERAL OPEN BAMACDE
RP COMPLEX, 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. Nonessential member of the complex that
CC stabilizes the interaction between the essential proteins BamA and
CC BamD. 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 PubMed:26744406). {ECO:0000269|PubMed:20378773,
CC ECO:0000269|PubMed:21823654, ECO:0000269|PubMed:22178970,
CC ECO:0000269|PubMed:26744406, ECO:0000269|PubMed:26900875,
CC ECO:0000269|PubMed:26901871, 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 Forms a subcomplex with BamD and BamE. 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 PubMed:26744406). {ECO:0000269|PubMed:15851030,
CC ECO:0000269|PubMed:16079137, 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 -!- INTERACTION:
CC P0A903; P0A903: bamC; NbExp=2; IntAct=EBI-1129043, EBI-1129043;
CC P0A903; P0AC02: bamD; NbExp=4; IntAct=EBI-1129043, EBI-1128087;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00924, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_00924, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:27686148}.
CC -!- DOMAIN: Contains two well-defined domains connected by a flexible
CC linker. The C-terminal domain may serve as an important protein-binding
CC surface for interaction with other Bam components or substrates. In
CC addition, contains a long unstructured N-terminal region, which is
CC required to stabilize the BamCD complex. Only the N-terminus of this
CC protein is observed in the Bam complex in X-ray or EM structures, most
CC of the protein must be highly mobile (PubMed:26900875, PubMed:26901871,
CC PubMed:27686148, PubMed:26744406). {ECO:0000269|PubMed:21624375,
CC ECO:0000269|PubMed:21937441, ECO:0000269|PubMed:22102230,
CC ECO:0000269|PubMed:26744406, ECO:0000269|PubMed:26900875,
CC ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:27686148}.
CC -!- MASS SPECTROMETRY: Mass=35163; Method=Electrospray; Note=With 3
CC palmitic acid (C16) acyl chains.;
CC Evidence={ECO:0000269|PubMed:27686148};
CC -!- MASS SPECTROMETRY: Mass=35183; 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 BamC family. {ECO:0000255|HAMAP-
CC Rule:MF_00924}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M33928; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X57402; CAA40661.1; -; Genomic_DNA.
DR EMBL; M33928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC75530.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16354.1; -; Genomic_DNA.
DR PIR; D65023; D65023.
DR RefSeq; NP_416972.4; NC_000913.3.
DR RefSeq; WP_001297320.1; NZ_STEB01000011.1.
DR PDB; 2LAE; NMR; -; A=101-344.
DR PDB; 2LAF; NMR; -; A=101-344.
DR PDB; 2YH5; X-ray; 1.25 A; A=226-344.
DR PDB; 2YH6; X-ray; 1.55 A; A/B/C/D=101-212.
DR PDB; 3SNS; X-ray; 1.50 A; A=224-343.
DR PDB; 3TGO; X-ray; 2.90 A; C/D=26-344.
DR PDB; 5AYW; X-ray; 3.56 A; C=33-88.
DR PDB; 5D0O; X-ray; 2.90 A; C=1-344.
DR PDB; 5D0Q; X-ray; 3.50 A; C/G=1-344.
DR PDB; 5EKQ; X-ray; 3.39 A; C=25-344.
DR PDB; 5LJO; EM; 4.90 A; C=25-189.
DR PDB; 6LYQ; X-ray; 3.19 A; C=1-344.
DR PDB; 6LYR; X-ray; 3.28 A; C=1-344.
DR PDB; 6LYS; X-ray; 3.05 A; C=1-344.
DR PDB; 6LYU; EM; 4.20 A; C=1-344.
DR PDB; 6SMX; EM; 6.65 A; C=25-83.
DR PDB; 6SN0; EM; 10.80 A; C=25-83.
DR PDB; 6SN2; EM; 9.50 A; C=25-83.
DR PDB; 6SN3; EM; 8.40 A; C=25-83.
DR PDB; 6SN4; EM; 9.50 A; C=25-83.
DR PDB; 6SN5; EM; 9.80 A; C=25-83.
DR PDB; 6SN7; EM; 8.90 A; C=25-83.
DR PDB; 6SN8; EM; 8.40 A; C=25-83.
DR PDB; 6SN9; EM; 9.80 A; C=25-83.
DR PDB; 6SO7; EM; 10.50 A; C=25-83.
DR PDB; 6SO8; EM; 9.80 A; C=25-83.
DR PDB; 6SOA; EM; 10.80 A; C=25-83.
DR PDB; 6SOB; EM; 8.50 A; C=25-83.
DR PDB; 6SOC; EM; 9.00 A; C=25-83.
DR PDB; 6SOG; EM; 8.30 A; C=25-83.
DR PDB; 6SOH; EM; 9.50 A; C=25-83.
DR PDB; 6SOJ; EM; 10.40 A; C=25-83.
DR PDB; 6V05; EM; 4.10 A; C=1-344.
DR PDB; 7BNQ; EM; 4.10 A; C=1-344.
DR PDB; 7NBX; EM; 4.80 A; C=1-344.
DR PDB; 7NCS; EM; 7.10 A; C=1-344.
DR PDB; 7ND0; EM; 5.20 A; C=1-344.
DR PDB; 7NRI; EM; 3.03 A; C=25-344.
DR PDBsum; 2LAE; -.
DR PDBsum; 2LAF; -.
DR PDBsum; 2YH5; -.
DR PDBsum; 2YH6; -.
DR PDBsum; 3SNS; -.
DR PDBsum; 3TGO; -.
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; 6V05; -.
DR PDBsum; 7BNQ; -.
DR PDBsum; 7NBX; -.
DR PDBsum; 7NCS; -.
DR PDBsum; 7ND0; -.
DR PDBsum; 7NRI; -.
DR AlphaFoldDB; P0A903; -.
DR BMRB; P0A903; -.
DR SMR; P0A903; -.
DR BioGRID; 4262898; 311.
DR ComplexPortal; CPX-1923; BAM complex.
DR DIP; DIP-39898N; -.
DR IntAct; P0A903; 8.
DR STRING; 511145.b2477; -.
DR TCDB; 1.B.33.1.3; the outer membrane protein insertion porin (bam complex) (ompip) family.
DR SWISS-2DPAGE; P0A903; -.
DR jPOST; P0A903; -.
DR PaxDb; P0A903; -.
DR PRIDE; P0A903; -.
DR DNASU; 946954; -.
DR EnsemblBacteria; AAC75530; AAC75530; b2477.
DR EnsemblBacteria; BAA16354; BAA16354; BAA16354.
DR GeneID; 66673658; -.
DR GeneID; 946954; -.
DR KEGG; ecj:JW2462; -.
DR KEGG; eco:b2477; -.
DR PATRIC; fig|1411691.4.peg.4262; -.
DR EchoBASE; EB0652; -.
DR eggNOG; COG3317; Bacteria.
DR HOGENOM; CLU_063217_1_0_6; -.
DR OMA; YTVVWDR; -.
DR PhylomeDB; P0A903; -.
DR BioCyc; EcoCyc:EG10658-MON; -.
DR EvolutionaryTrace; P0A903; -.
DR PRO; PR:P0A903; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990063; C:Bam protein complex; IDA:EcoCyc.
DR GO; GO:0009986; C:cell surface; 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 DisProt; DP01339; -.
DR Gene3D; 3.30.310.170; -; 1.
DR HAMAP; MF_00924; OM_assembly_BamC; 1.
DR InterPro; IPR014524; BamC.
DR InterPro; IPR042268; BamC_C.
DR InterPro; IPR010653; NlpB/DapX.
DR Pfam; PF06804; Lipoprotein_18; 1.
DR PIRSF; PIRSF026343; NlpB; 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..24
FT CHAIN 25..344
FT /note="Outer membrane protein assembly factor BamC"
FT /id="PRO_0000018027"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00924,
FT ECO:0000269|PubMed:1885529, ECO:0000305|PubMed:27686148"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00924,
FT ECO:0000269|PubMed:1885529, ECO:0000305|PubMed:27686148"
FT CONFLICT 219
FT /note="A -> R (in Ref. 2; M33928)"
FT /evidence="ECO:0000305"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:3TGO"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:5D0O"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:3TGO"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6LYQ"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3TGO"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3TGO"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2YH6"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:2LAF"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:2YH6"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2YH6"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2YH6"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2YH6"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2YH6"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2YH6"
FT STRAND 157..168
FT /evidence="ECO:0007829|PDB:2YH6"
FT STRAND 171..183
FT /evidence="ECO:0007829|PDB:2YH6"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2YH6"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:2YH6"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:2YH5"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5D0Q"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:2YH5"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:2YH5"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:2YH5"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2YH5"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2YH5"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:2YH5"
FT STRAND 300..310
FT /evidence="ECO:0007829|PDB:2YH5"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:2YH5"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5D0Q"
FT HELIX 328..344
FT /evidence="ECO:0007829|PDB:2YH5"
SQ SEQUENCE 344 AA; 36842 MW; 49991F277D9D923C CRC64;
MAYSVQKSRL AKVAGVSLVL LLAACSSDSR YKRQVSGDEA YLEAAPLAEL HAPAGMILPV
TSGDYAIPVT NGSGAVGKAL DIRPPAQPLA LVSGARTQFT GDTASLLVEN GRGNTLWPQV
VSVLQAKNYT ITQRDDAGQT LTTDWVQWNR LDEDEQYRGR YQISVKPQGY QQAVTVKLLN
LEQAGKPVAD AASMQRYSTE MMNVISAGLD KSATDAANAA QNRASTTMDV QSAADDTGLP
MLVVRGPFNV VWQRLPAALE KVGMKVTDST RSQGNMAVTY KPLSDSDWQE LGASDPGLAS
GDYKLQVGDL DNRSSLQFID PKGHTLTQSQ NDALVAVFQA AFSK
