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Protein

Outer membrane protein assembly factor BamA

Gene

bamA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • cell adhesion Source: UniProtKB-KW
  • Gram-negative-bacterium-type cell outer membrane assembly Source: EcoCyc
  • protein insertion into membrane Source: EcoCyc

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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

  • Bam protein complex Source: EcoCyc
  • cell outer membrane Source: EcoCyc
  • integral component of membrane Source: UniProtKB-KW

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

PaxDbiP0A940.
PRIDEiP0A940.

2D gel databases

SWISS-2DPAGEiP0A940.

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

Show more details

Protein-protein interaction databases

BioGridi4259504. 695 interactors.
DIPiDIP-36019N.
IntActiP0A940. 14 interactors.
STRINGi316385.ECDH10B_0157.

Structurei

Secondary structure

1810
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 33Combined sources6
Beta strandi35 – 37Combined sources3
Helixi39 – 44Combined sources6
Helixi56 – 67Combined sources12
Beta strandi72 – 80Combined sources9
Beta strandi83 – 90Combined sources8
Beta strandi93 – 101Combined sources9
Beta strandi103 – 105Combined sources3
Helixi107 – 115Combined sources9
Turni116 – 118Combined sources3
Beta strandi121 – 123Combined sources3
Helixi127 – 129Combined sources3
Helixi130 – 140Combined sources11
Helixi141 – 144Combined sources4
Beta strandi146 – 148Combined sources3
Beta strandi150 – 158Combined sources9
Turni159 – 161Combined sources3
Beta strandi162 – 170Combined sources9
Beta strandi176 – 184Combined sources9
Beta strandi186 – 188Combined sources3
Helixi190 – 194Combined sources5
Helixi195 – 197Combined sources3
Turni210 – 212Combined sources3
Helixi216 – 231Combined sources16
Turni232 – 234Combined sources3
Beta strandi239 – 247Combined sources9
Beta strandi251 – 261Combined sources11
Beta strandi267 – 276Combined sources10
Turni278 – 280Combined sources3
Helixi281 – 287Combined sources7
Helixi298 – 313Combined sources16
Turni314 – 316Combined sources3
Beta strandi317 – 319Combined sources3
Beta strandi321 – 329Combined sources9
Turni330 – 333Combined sources4
Beta strandi334 – 342Combined sources9
Beta strandi348 – 356Combined sources9
Beta strandi358 – 360Combined sources3
Helixi362 – 366Combined sources5
Beta strandi373 – 376Combined sources4
Helixi379 – 392Combined sources14
Beta strandi396 – 405Combined sources10
Beta strandi408 – 419Combined sources12
Beta strandi427 – 433Combined sources7
Turni434 – 436Combined sources3
Beta strandi437 – 453Combined sources17
Beta strandi455 – 462Combined sources8
Beta strandi464 – 475Combined sources12
Turni479 – 482Combined sources4
Beta strandi484 – 495Combined sources12
Helixi496 – 499Combined sources4
Beta strandi501 – 503Combined sources3
Beta strandi505 – 520Combined sources16
Beta strandi523 – 537Combined sources15
Helixi543 – 551Combined sources9
Beta strandi558 – 561Combined sources4
Beta strandi564 – 579Combined sources16
Beta strandi584 – 586Combined sources3
Beta strandi589 – 600Combined sources12
Beta strandi604 – 606Combined sources3
Beta strandi608 – 620Combined sources13
Beta strandi622 – 625Combined sources4
Beta strandi627 – 643Combined sources17
Helixi648 – 650Combined sources3
Beta strandi656 – 660Combined sources5
Beta strandi671 – 674Combined sources4
Beta strandi685 – 687Combined sources3
Beta strandi689 – 691Combined sources3
Helixi692 – 694Combined sources3
Beta strandi700 – 705Combined sources6
Beta strandi708 – 720Combined sources13
Beta strandi723 – 725Combined sources3
Turni727 – 731Combined sources5
Beta strandi733 – 745Combined sources13
Turni751 – 756Combined sources6
Beta strandi767 – 778Combined sources12
Beta strandi781 – 792Combined sources12
Beta strandi802 – 809Combined sources8

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...

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.
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.
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

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: September 27, 2017
This is version 117 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families