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UniProtKB - P0A940 (BAMA_ECOLI)

Protein

Outer membrane protein assembly factor BamA

Gene

bamA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits (PubMed:20378773, PubMed:21823654, PubMed:27686148). A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406).9 Publications
Acts as a receptor for CdiA-EC93, the contact-dependent growth inhibition (CDI) effector of E.coli strain EC93; antibodies against extracellular epitopes decrease CDI. Its role in CDI is independent of the other Bam complex components (PubMed:18761695). Also acts as a receptor for CDI with CdiA from E.coli strain 536 / UPEC, which does not have the same mode of toxicity as CdiA from strain EC93 (PubMed:23469034, PubMed:23882017). Susceptibility to CdiA-EC93 is dependent on E.coli BamA; replacing BamA with the gene from S.typhimurium LT2, E.cloacae ATCC 13047 or D.dadantii 3937 renders cells resistant to CdiA-EC93. Cells with BamA from another bacteria no longer form CdiA-EC93-induced aggregates with EC93 cells. A chimera in which E.cloacae extracellular loops 6 and 7 are replaced with loops 6 and 7 from E.coli is susceptible to CdiA-EC93 and to CdiA-CT from strain 536 / UPEC (PubMed:23882017).3 Publications

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

BioCyciEcoCyc:G6093-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Outer membrane protein assembly factor BamAUniRule annotation
Alternative name(s):
Omp85
Gene namesi
Name:bamAUniRule annotation
Synonyms:yaeT, yzzN, yzzY
Ordered Locus Names:b0177, JW0172
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12676 bamA

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 424PeriplasmicCuratedAdd BLAST404
Transmembranei425 – 433Beta stranded; Name=Strand 11 Publication9
Topological domaini434 – 435Extracellular; loop 1Curated2
Transmembranei436 – 446Beta stranded; Name=Strand 21 PublicationAdd BLAST11
Topological domaini447 – 454PeriplasmicCurated8
Transmembranei455 – 462Beta stranded; Name=Strand 31 Publication8
Topological domaini463 – 465Extracellular; loop 2Curated3
Transmembranei466 – 475Beta stranded; Name=Strand 41 Publication10
Topological domaini476 – 483PeriplasmicCurated8
Transmembranei484 – 495Beta stranded; Name=Strand 51 PublicationAdd BLAST12
Topological domaini496 – 504Extracellular; loop 3Curated9
Transmembranei505 – 506Beta stranded; Name=Strand 61 Publication2
Topological domaini507 – 522PeriplasmicCuratedAdd BLAST16
Transmembranei523 – 535Beta stranded; Name=Strand 71 PublicationAdd BLAST13
Topological domaini536 – 563Extracellular; loop 42 PublicationsAdd BLAST28
Transmembranei564 – 577Beta stranded; Name=Strand 81 PublicationAdd BLAST14
Topological domaini578 – 590PeriplasmicCuratedAdd BLAST13
Transmembranei591 – 600Beta stranded; Name=Strand 91 Publication10
Topological domaini601 – 608Extracellular; loop 5Curated8
Transmembranei609 – 619Beta stranded; Name=Strand 101 PublicationAdd BLAST11
Topological domaini620 – 628PeriplasmicCurated9
Transmembranei629 – 639Beta stranded; Name=Strand 111 PublicationAdd BLAST11
Topological domaini640 – 708Extracellular; loop 62 PublicationsAdd BLAST69
Transmembranei709 – 718Beta stranded; Name=Strand 121 Publication10
Topological domaini719 – 732PeriplasmicCuratedAdd BLAST14
Transmembranei733 – 745Beta stranded; Name=Strand 131 PublicationAdd BLAST13
Topological domaini746 – 767Extracellular; loop 7CuratedAdd BLAST22
Transmembranei768 – 777Beta stranded; Name=Strand 141 Publication10
Topological domaini778PeriplasmicCurated1
Transmembranei779 – 789Beta stranded; Name=Strand 151 PublicationAdd BLAST11
Topological domaini790 – 803Extracellular; loop 8CuratedAdd BLAST14
Transmembranei804 – 808Beta stranded; Name=Strand 161 Publication5

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Deletion is lethal. Depletion results in the accumulation of incorrectly assembled outer membrane proteins, including TolC, OmpF, OmpC and OmpA (PubMed:15851030, PubMed:16102012). Decreased expression leads to decreased susceptibility to contact-dependent growth inhibition (CDI), and decreased expression of outer membrane proteins (including in this study LamB) as well as up-regulation of periplasmic protease DegP (PubMed:18761695, PubMed:23469034).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi181N → A: Lethal, protein does not accumulate. 1 Publication1
Mutagenesisi251K → A: Lethal, protein does not accumulate. 1 Publication1
Mutagenesisi259N → A: Lethal, protein does not accumulate. 1 Publication1
Mutagenesisi351 – 353KIR → PIP: Lethal, wild-type protein levels. 1 Publication3
Mutagenesisi351K → P: Reduces cell growth, wild-type protein levels. 1 Publication1
Mutagenesisi366R → E: Severely impairs cell growth, wild-type protein levels. 1 Publication1
Mutagenesisi373E → K: Lethal, wild-type protein levels. 2 Publications1
Mutagenesisi393G → C: No effect. Lethal; when associated with C-584, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi415 – 419VYKVK → PYKVP: Lethal, wild-type protein levels. 1 Publication5
Mutagenesisi415 – 417VYK → PYP: Lethal, wild-type protein levels. 1 Publication3
Mutagenesisi417 – 419KVK → PVP: Lethal, wild-type protein levels. 1 Publication3
Mutagenesisi429G → P: Lethal, wild-type protein levels. 1 Publication1
Mutagenesisi430I → C: Reduced folding of OmpT; when associated with C-808, traps protein in lateral closed conformation, growth restored by reducing agent. 1 Publication1
Mutagenesisi435E → C: No effect. Lethal; when associated with C-658 or C-665, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi435E → L: Very minor growth defect. Lethal; when associated with L-800. 1 Publication1
Mutagenesisi464D → L: Very minor growth defect. 1 Publication1
Mutagenesisi500D → L: Very minor growth defect. 1 Publication1
Mutagenesisi547R → A: Lethal. 1 Publication1
Mutagenesisi554 – 562EHPSTSDQD → VDYPYDVPDYA: Loop 4 to HA epitope; still susceptible to CdiA-EC93. 1 Publication9
Mutagenesisi556 – 563PSTSDQDN → G: Delta loop 4; slight increase in resistance to CdiA-EC93, forms aggregates with CdiA-EC93 cells. 1 Publication8
Mutagenesisi584G → C: No effect. Lethal; when associated with C-393, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi658S → C: No effect. Lethal; when associated with C-435, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi661R → A: Slow growth on solid and liquid media, less protein accumulates which is more proteinase sensitive. 1 Publication1
Mutagenesisi665S → C: No effect. Lethal; when associated with C-435, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi673 – 702Missing : Lethal. 1 PublicationAdd BLAST30
Mutagenesisi675 – 701FPHQA…KDLCK → G: Delta loop 6; fully resistant to CdiA-EC93, does not form aggregates with CdiA-EC93 cells. 1 PublicationAdd BLAST27
Mutagenesisi677 – 685HQASNYDPD → VDYPYDVPDYA: Loop 6 to HA epitope; still susceptible to CdiA-EC93. 1 Publication9
Mutagenesisi740D → A: Slow growth on solid and liquid media, less protein accumulates which is more proteinase sensitive. 1 Publication1
Mutagenesisi754 – 755YS → VDYPYDVPDYA: Loop 7 to HA epitope; fully resistant to CdiA-EC93, does not form aggregates with CdiA-EC93 cells. 1 Publication2
Mutagenesisi800E → L: Very minor growth defect. Lethal; when associated with L-435. 1 Publication1
Mutagenesisi808K → C: Reduced folding of OmpT; when associated with C-430, traps protein in lateral closed conformation, growth restored by reducing agent. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20UniRule annotation1 PublicationAdd BLAST20
ChainiPRO_000003347021 – 810Outer membrane protein assembly factor BamAAdd BLAST790

Proteomic databases

EPDiP0A940
PaxDbiP0A940
PRIDEiP0A940

2D gel databases

SWISS-2DPAGEiP0A940

PTM databases

CarbonylDBiP0A940

Interactioni

Subunit structurei

Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. BamA interacts directly with BamB and the BamCDE subcomplex. The Bam complex has the shape of a hat, with the BamA beta-barrel crown in the outer membrane and the periplasmic brim formed by the BamA POTRA domains and the 4 lipoproteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406).10 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi4259504, 747 interactors
ComplexPortaliCPX-1923 Bam complex
DIPiDIP-36019N
IntActiP0A940, 14 interactors
STRINGi316385.ECDH10B_0157

Structurei

Secondary structure

1810
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A940
SMRiP0A940
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A940

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 91POTRA 1PROSITE-ProRule annotation1 PublicationAdd BLAST68
Domaini92 – 172POTRA 2PROSITE-ProRule annotation1 PublicationAdd BLAST81
Domaini175 – 263POTRA 3PROSITE-ProRule annotation1 PublicationAdd BLAST89
Domaini266 – 344POTRA 4PROSITE-ProRule annotation1 PublicationAdd BLAST79
Domaini347 – 421POTRA 5PROSITE-ProRule annotation1 PublicationAdd BLAST75

Domaini

Contains 5 N-terminal periplasmic polypeptide transport-associated (POTRA) domains which interact with other subunits of the complex, may recruit substrates from the periplasm into the outer membrane and also act as a chaperone (PubMed:17702946, PubMed:18430136, PubMed:19081063, PubMed:21795783, PubMed:14559180). The C-terminal region forms a discontinuous 16-stranded beta-barrel transmembrane region. The central pore is ellipsoid, and probably closed by extracellular loop 6, perhaps with the aid of other loops (PubMed:24914988, PubMed:24619089).1 Publication6 Publications

Sequence similaritiesi

Belongs to the BamA family.UniRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105E1Z Bacteria
COG4775 LUCA
InParanoidiP0A940
KOiK07277
OMAiGGFNSVR
PhylomeDBiP0A940

Family and domain databases

HAMAPiMF_01430 OM_assembly_BamA, 1 hit
InterProiView protein in InterPro
IPR000184 Bac_surfAg_D15
IPR010827 BamA/TamA_POTRA
IPR023707 OM_assembly_BamA
IPR034746 POTRA
PANTHERiPTHR12815:SF23 PTHR12815:SF23, 1 hit
PfamiView protein in Pfam
PF01103 Bac_surface_Ag, 1 hit
PF07244 POTRA, 4 hits
PIRSFiPIRSF006076 OM_assembly_OMP85, 1 hit
TIGRFAMsiTIGR03303 OM_YaeT, 1 hit
PROSITEiView protein in PROSITE
PS51779 POTRA, 5 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A940-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAMKKLLIAS LLFSSATVYG AEGFVVKDIH FEGLQRVAVG AALLSMPVRT 
        60         70         80         90        100
GDTVNDEDIS NTIRALFATG NFEDVRVLRD GDTLLVQVKE RPTIASITFS 
       110        120        130        140        150
GNKSVKDDML KQNLEASGVR VGESLDRTTI ADIEKGLEDF YYSVGKYSAS 
       160        170        180        190        200
VKAVVTPLPR NRVDLKLVFQ EGVSAEIQQI NIVGNHAFTT DELISHFQLR 
       210        220        230        240        250
DEVPWWNVVG DRKYQKQKLA GDLETLRSYY LDRGYARFNI DSTQVSLTPD 
       260        270        280        290        300
KKGIYVTVNI TEGDQYKLSG VEVSGNLAGH SAEIEQLTKI EPGELYNGTK 
       310        320        330        340        350
VTKMEDDIKK LLGRYGYAYP RVQSMPEIND ADKTVKLRVN VDAGNRFYVR 
       360        370        380        390        400
KIRFEGNDTS KDAVLRREMR QMEGAWLGSD LVDQGKERLN RLGFFETVDT 
       410        420        430        440        450
DTQRVPGSPD QVDVVYKVKE RNTGSFNFGI GYGTESGVSF QAGVQQDNWL 
       460        470        480        490        500
GTGYAVGING TKNDYQTYAE LSVTNPYFTV DGVSLGGRLF YNDFQADDAD 
       510        520        530        540        550
LSDYTNKSYG TDVTLGFPIN EYNSLRAGLG YVHNSLSNMQ PQVAMWRYLY 
       560        570        580        590        600
SMGEHPSTSD QDNSFKTDDF TFNYGWTYNK LDRGYFPTDG SRVNLTGKVT 
       610        620        630        640        650
IPGSDNEYYK VTLDTATYVP IDDDHKWVVL GRTRWGYGDG LGGKEMPFYE 
       660        670        680        690        700
NFYAGGSSTV RGFQSNTIGP KAVYFPHQAS NYDPDYDYEC ATQDGAKDLC 
       710        720        730        740        750
KSDDAVGGNA MAVASLEFIT PTPFISDKYA NSVRTSFFWD MGTVWDTNWD 
       760        770        780        790        800
SSQYSGYPDY SDPSNIRMSA GIALQWMSPL GPLVFSYAQP FKKYDGDKAE 
       810
QFQFNIGKTW
Length:810
Mass (Da):90,553
Last modified:July 19, 2005 - v1
Checksum:iDDCE4C6D341664EB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115E → Q in AAK64508 (Ref. 2) Curated1
Sequence conflicti228S → I in AAK64508 (Ref. 2) Curated1
Sequence conflicti361K → R in AAK64508 (Ref. 2) Curated1
Sequence conflicti632R → C in AAK64508 (Ref. 2) Curated1
Sequence conflicti712A → T in AAK64508 (Ref. 2) Curated1

Mass spectrometryi

Molecular mass is 88426 Da from positions 21 - 810. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF407013 Genomic DNA Translation: AAL01379.1
AY035865 Genomic DNA Translation: AAK64508.1
U70214 Genomic DNA Translation: AAB08606.1
U00096 Genomic DNA Translation: AAC73288.1
AP009048 Genomic DNA Translation: BAA77852.2
PIRiA64742
RefSeqiNP_414719.1, NC_000913.3
WP_001240896.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73288; AAC73288; b0177
BAA77852; BAA77852; BAA77852
GeneIDi944870
KEGGiecj:JW0172
eco:b0177
PATRICifig|1411691.4.peg.2102

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF407013 Genomic DNA Translation: AAL01379.1
AY035865 Genomic DNA Translation: AAK64508.1
U70214 Genomic DNA Translation: AAB08606.1
U00096 Genomic DNA Translation: AAC73288.1
AP009048 Genomic DNA Translation: BAA77852.2
PIRiA64742
RefSeqiNP_414719.1, NC_000913.3
WP_001240896.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QCZX-ray2.70A/B21-351[»]
2QDFX-ray2.20A21-351[»]
2V9HNMR-A21-184[»]
3EFCX-ray3.30A21-410[»]
3OG5X-ray2.69A/B264-424[»]
3Q6BX-ray1.50A266-420[»]
4C4VX-ray3.00A347-810[»]
B344-810[»]
4N75X-ray2.60A/B427-810[»]
4PK1X-ray3.10A175-424[»]
4XGAX-ray2.15B175-420[»]
5AYWX-ray3.56A22-810[»]
5D0OX-ray2.90A1-810[»]
5D0QX-ray3.50A/F1-810[»]
5EKQX-ray3.39A21-810[»]
5LJOelectron microscopy4.90A24-806[»]
ProteinModelPortaliP0A940
SMRiP0A940
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259504, 747 interactors
ComplexPortaliCPX-1923 Bam complex
DIPiDIP-36019N
IntActiP0A940, 14 interactors
STRINGi316385.ECDH10B_0157

PTM databases

CarbonylDBiP0A940

2D gel databases

SWISS-2DPAGEiP0A940

Proteomic databases

EPDiP0A940
PaxDbiP0A940
PRIDEiP0A940

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73288; AAC73288; b0177
BAA77852; BAA77852; BAA77852
GeneIDi944870
KEGGiecj:JW0172
eco:b0177
PATRICifig|1411691.4.peg.2102

Organism-specific databases

EchoBASEiEB2541
EcoGeneiEG12676 bamA

Phylogenomic databases

eggNOGiENOG4105E1Z Bacteria
COG4775 LUCA
InParanoidiP0A940
KOiK07277
OMAiGGFNSVR
PhylomeDBiP0A940

Enzyme and pathway databases

BioCyciEcoCyc:G6093-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A940
PROiPR:P0A940

Family and domain databases

HAMAPiMF_01430 OM_assembly_BamA, 1 hit
InterProiView protein in InterPro
IPR000184 Bac_surfAg_D15
IPR010827 BamA/TamA_POTRA
IPR023707 OM_assembly_BamA
IPR034746 POTRA
PANTHERiPTHR12815:SF23 PTHR12815:SF23, 1 hit
PfamiView protein in Pfam
PF01103 Bac_surface_Ag, 1 hit
PF07244 POTRA, 4 hits
PIRSFiPIRSF006076 OM_assembly_OMP85, 1 hit
TIGRFAMsiTIGR03303 OM_YaeT, 1 hit
PROSITEiView protein in PROSITE
PS51779 POTRA, 5 hits
ProtoNetiSearch...

Entry informationi

Entry nameiBAMA_ECOLI
AccessioniPrimary (citable) accession number: P0A940
Secondary accession number(s): P39170
, P39181, P77465, Q548B8, Q8KR94, Q9R2E3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: June 20, 2018
This is version 123 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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