BAME_ECOLI
ID BAME_ECOLI Reviewed; 113 AA.
AC P0A937; P23089;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Outer membrane protein assembly factor BamE {ECO:0000255|HAMAP-Rule:MF_00925};
DE Flags: Precursor;
GN Name=bamE {ECO:0000255|HAMAP-Rule:MF_00925}; Synonyms=smpA;
GN OrderedLocusNames=b2617, JW2598;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-113.
RC STRAIN=K12;
RX PubMed=2045357; DOI=10.1128/jb.173.11.3271-3272.1991;
RA Chauhan A.K., Miczak A., Apirion D.;
RT "Two new genes located between 2758 and 2761 kilobase pairs on the
RT Escherichia coli genome.";
RL J. Bacteriol. 173:3271-3272(1991).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [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]
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 [9]
RP CRYSTALLIZATION, AND SUBUNIT.
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 [10] {ECO:0007744|PDB:2KXX}
RP STRUCTURE BY NMR OF 21-113, FUNCTION, AND SUBUNIT.
RX PubMed=21207987; DOI=10.1021/bi101659u;
RA Kim K.H., Kang H.S., Okon M., Escobar-Cabrera E., McIntosh L.P.,
RA Paetzel M.;
RT "Structural characterization of Escherichia coli BamE, a lipoprotein
RT component of the beta-barrel assembly machinery complex.";
RL Biochemistry 50:1081-1090(2011).
RN [11] {ECO:0007744|PDB:2KM7}
RP STRUCTURE BY NMR OF 21-113, AND SUBUNIT.
RX PubMed=21212804; DOI=10.1038/embor.2010.202;
RA Knowles T.J., Browning D.F., Jeeves M., Maderbocus R., Rajesh S.,
RA Sridhar P., Manoli E., Emery D., Sommer U., Spencer A., Leyton D.L.,
RA Squire D., Chaudhuri R.R., Viant M.R., Cunningham A.F., Henderson I.R.,
RA Overduin M.;
RT "Structure and function of BamE within the outer membrane and the beta-
RT barrel assembly machine.";
RL EMBO Rep. 12:123-128(2011).
RN [12] {ECO:0007744|PDB:2YH9}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 34-113, 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 [13] {ECO:0007744|PDB:5LJO}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 24-110 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 [14] {ECO:0007744|PDB:5AYW}
RP X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 20-113 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 [15] {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 [16] {ECO:0007744|PDB:5EKQ}
RP X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 20-113 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. May modulate the conformation of BamA, likely through
CC interactions with BamD. 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:17404237,
CC ECO:0000269|PubMed:20378773, ECO:0000269|PubMed:21207987,
CC ECO:0000269|PubMed:21586578, ECO:0000269|PubMed:21823654,
CC ECO:0000269|PubMed:22178970, ECO:0000269|PubMed:26744406,
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 Forms a subcomplex with BamC and BamD. Monomer in the periplasm, but is
CC able to adopt a dimeric conformation in the cytoplasm
CC (PubMed:21207987). The Bam complex has the shape of a hat, with the
CC BamA beta-barrel crown in the outer membrane and the periplasmic brim
CC formed by the BamA POTRA domains and the 4 lipoproteins
CC (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406).
CC The intact Bam complex can have 2 BamE subunits (PubMed:27686148).
CC {ECO:0000269|PubMed:17404237, ECO:0000269|PubMed:20378773,
CC ECO:0000269|PubMed:21139201, ECO:0000269|PubMed:21207987,
CC ECO:0000269|PubMed:21212804, ECO:0000269|PubMed:21586578,
CC ECO:0000269|PubMed:21823654, ECO:0000269|PubMed:26744406,
CC ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871,
CC ECO:0000269|PubMed:27686148}.
CC -!- INTERACTION:
CC P0A937; P0AC02: bamD; NbExp=3; IntAct=EBI-6391574, EBI-1128087;
CC P0A937; P0A937: bamE; NbExp=14; IntAct=EBI-6391574, EBI-6391574;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00925, ECO:0000269|PubMed:17404237,
CC ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_00925, ECO:0000269|PubMed:17404237,
CC ECO:0000269|PubMed:27686148}.
CC -!- MASS SPECTROMETRY: Mass=12383; Method=Electrospray; Note=With 3
CC palmitic acid (C16) acyl chains.;
CC Evidence={ECO:0000269|PubMed:27686148};
CC -!- MASS SPECTROMETRY: Mass=12413; Method=Electrospray; Note=With 2
CC palmitic (C16) and 1 stearic (C18) acid acyl chains.;
CC Evidence={ECO:0000269|PubMed:27686148};
CC -!- DISRUPTION PHENOTYPE: Mutants show minor defects in the assembly of
CC outer membrane proteins. {ECO:0000269|PubMed:17404237}.
CC -!- SIMILARITY: Belongs to the BamE family. {ECO:0000255|HAMAP-
CC Rule:MF_00925}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA36847.1; Type=Miscellaneous discrepancy; Note=Sequence of unknown provenance, it does not match this entry.; Evidence={ECO:0000305};
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DR EMBL; U36840; AAA79787.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75666.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16502.1; -; Genomic_DNA.
DR EMBL; X52620; CAA36847.1; ALT_SEQ; Genomic_DNA.
DR PIR; S11646; S11646.
DR PIR; T08630; T08630.
DR RefSeq; NP_417107.2; NC_000913.3.
DR RefSeq; WP_001203437.1; NZ_STEB01000040.1.
DR PDB; 2KM7; NMR; -; A=20-113.
DR PDB; 2KXX; NMR; -; A=21-113.
DR PDB; 2YH9; X-ray; 1.80 A; A/B/C=34-113.
DR PDB; 5AYW; X-ray; 3.56 A; E=20-113.
DR PDB; 5D0O; X-ray; 2.90 A; E=1-113.
DR PDB; 5D0Q; X-ray; 3.50 A; E/I=1-113.
DR PDB; 5EKQ; X-ray; 3.39 A; E=20-113.
DR PDB; 5LJO; EM; 4.90 A; E=24-110.
DR PDB; 6LYQ; X-ray; 3.19 A; E=1-113.
DR PDB; 6LYR; X-ray; 3.28 A; E=1-113.
DR PDB; 6LYS; X-ray; 3.05 A; E=1-113.
DR PDB; 6LYU; EM; 4.20 A; E=1-113.
DR PDB; 6SMX; EM; 6.65 A; E=24-110.
DR PDB; 6SN0; EM; 10.80 A; E=24-110.
DR PDB; 6SN2; EM; 9.50 A; E=24-110.
DR PDB; 6SN3; EM; 8.40 A; E=24-110.
DR PDB; 6SN4; EM; 9.50 A; E=24-110.
DR PDB; 6SN5; EM; 9.80 A; E=24-110.
DR PDB; 6SN7; EM; 8.90 A; E=24-110.
DR PDB; 6SN8; EM; 8.40 A; E=24-110.
DR PDB; 6SN9; EM; 9.80 A; E=24-110.
DR PDB; 6SO7; EM; 10.50 A; E=24-110.
DR PDB; 6SO8; EM; 9.80 A; E=24-110.
DR PDB; 6SOA; EM; 10.80 A; E=24-110.
DR PDB; 6SOB; EM; 8.50 A; E=24-110.
DR PDB; 6SOC; EM; 9.00 A; E=24-110.
DR PDB; 6SOG; EM; 8.30 A; E=24-110.
DR PDB; 6SOH; EM; 9.50 A; E=24-110.
DR PDB; 6SOJ; EM; 10.40 A; E=24-110.
DR PDB; 6V05; EM; 4.10 A; E=1-113.
DR PDB; 7BNQ; EM; 4.10 A; E=1-113.
DR PDB; 7NBX; EM; 4.80 A; E=1-113.
DR PDB; 7NCS; EM; 7.10 A; E=1-113.
DR PDB; 7ND0; EM; 5.20 A; E=1-113.
DR PDB; 7NRI; EM; 3.03 A; E=20-113.
DR PDBsum; 2KM7; -.
DR PDBsum; 2KXX; -.
DR PDBsum; 2YH9; -.
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; P0A937; -.
DR BMRB; P0A937; -.
DR SMR; P0A937; -.
DR BioGRID; 4259570; 145.
DR BioGRID; 849957; 2.
DR ComplexPortal; CPX-1923; BAM complex.
DR DIP; DIP-10895N; -.
DR IntAct; P0A937; 6.
DR MINT; P0A937; -.
DR STRING; 511145.b2617; -.
DR TCDB; 1.B.33.1.3; the outer membrane protein insertion porin (bam complex) (ompip) family.
DR jPOST; P0A937; -.
DR PaxDb; P0A937; -.
DR PRIDE; P0A937; -.
DR EnsemblBacteria; AAC75666; AAC75666; b2617.
DR EnsemblBacteria; BAA16502; BAA16502; BAA16502.
DR GeneID; 66673495; -.
DR GeneID; 945583; -.
DR KEGG; ecj:JW2598; -.
DR KEGG; eco:b2617; -.
DR PATRIC; fig|1411691.4.peg.4122; -.
DR EchoBASE; EB0945; -.
DR eggNOG; COG2913; Bacteria.
DR HOGENOM; CLU_083835_4_0_6; -.
DR InParanoid; P0A937; -.
DR OMA; VWYYVFR; -.
DR PhylomeDB; P0A937; -.
DR BioCyc; EcoCyc:EG10952-MON; -.
DR EvolutionaryTrace; P0A937; -.
DR PRO; PR:P0A937; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990063; C:Bam protein complex; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:EcoCyc.
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 GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR Gene3D; 3.30.1450.10; -; 1.
DR HAMAP; MF_00925; OM_assembly_BamE; 1.
DR InterPro; IPR026592; BamE.
DR InterPro; IPR037873; BamE-like.
DR InterPro; IPR007450; Lipoprotein_SmpA/OmlA.
DR PANTHER; PTHR37482; PTHR37482; 1.
DR Pfam; PF04355; SmpA_OmlA; 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_00925"
FT CHAIN 20..113
FT /note="Outer membrane protein assembly factor BamE"
FT /id="PRO_0000032810"
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 STRAND 32..35
FT /evidence="ECO:0007829|PDB:5D0O"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:5D0O"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:2YH9"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2YH9"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5D0O"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2YH9"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5D0O"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2YH9"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2YH9"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:2YH9"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2KM7"
SQ SEQUENCE 113 AA; 12302 MW; CFD8840C014AA0A2 CRC64;
MRCKTLTAAA AVLLMLTAGC STLERVVYRP DINQGNYLTA NDVSKIRVGM TQQQVAYALG
TPLMSDPFGT NTWFYVFRQQ PGHEGVTQQT LTLTFNSSGV LTNIDNKPAL SGN
