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P0A940 (BAMA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Outer membrane protein assembly factor BamA
Alternative name(s):
Omp85
Gene names
Name:bamA
Synonyms:yaeT, yzzN, yzzY
Ordered Locus Names:b0177, JW0172
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the outer membrane protein assembly complex, 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. Ref.9 Ref.11 Ref.12 Ref.14 Ref.15

Subunit structure

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. Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

Cell outer membrane Ref.10.

Domain

Contains 5 N-terminal periplasmic polypeptide transport-associated (POTRA) domains and a C-terminal transmembrane region. POTRA domains interact with other subunits of the complex, may recruit substrates from the periplasm into the outer membrane and also act as a chaperone. Ref.17 Ref.18 Ref.19 Ref.20

Disruption phenotype

Depletion results in the accumulation of incorrectly assembled outer membrane proteins, including TolC, OmpF, OmpC and OmpA. Deletion is lethal. Ref.8 Ref.11

Sequence similarities

Belongs to the BamA family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

bamBP7777416EBI-907371,EBI-907297
bamDP0AC0213EBI-907371,EBI-1128087

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.7
Chain21 – 810790Outer membrane protein assembly factor BamA HAMAP-Rule MF_01430
PRO_0000033470

Experimental info

Sequence conflict1151E → Q in AAK64508. Ref.2
Sequence conflict2281S → I in AAK64508. Ref.2
Sequence conflict3611K → R in AAK64508. Ref.2
Sequence conflict6321R → C in AAK64508. Ref.2
Sequence conflict7121A → T in AAK64508. Ref.2

Secondary structure

........................................................................ 810
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A940 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: DDCE4C6D341664EB

FASTA81090,553
        10         20         30         40         50         60 
MAMKKLLIAS LLFSSATVYG AEGFVVKDIH FEGLQRVAVG AALLSMPVRT GDTVNDEDIS 

        70         80         90        100        110        120 
NTIRALFATG NFEDVRVLRD GDTLLVQVKE RPTIASITFS GNKSVKDDML KQNLEASGVR 

       130        140        150        160        170        180 
VGESLDRTTI ADIEKGLEDF YYSVGKYSAS VKAVVTPLPR NRVDLKLVFQ EGVSAEIQQI 

       190        200        210        220        230        240 
NIVGNHAFTT DELISHFQLR DEVPWWNVVG DRKYQKQKLA GDLETLRSYY LDRGYARFNI 

       250        260        270        280        290        300 
DSTQVSLTPD KKGIYVTVNI TEGDQYKLSG VEVSGNLAGH SAEIEQLTKI EPGELYNGTK 

       310        320        330        340        350        360 
VTKMEDDIKK LLGRYGYAYP RVQSMPEIND ADKTVKLRVN VDAGNRFYVR KIRFEGNDTS 

       370        380        390        400        410        420 
KDAVLRREMR QMEGAWLGSD LVDQGKERLN RLGFFETVDT DTQRVPGSPD QVDVVYKVKE 

       430        440        450        460        470        480 
RNTGSFNFGI GYGTESGVSF QAGVQQDNWL GTGYAVGING TKNDYQTYAE LSVTNPYFTV 

       490        500        510        520        530        540 
DGVSLGGRLF YNDFQADDAD LSDYTNKSYG TDVTLGFPIN EYNSLRAGLG YVHNSLSNMQ 

       550        560        570        580        590        600 
PQVAMWRYLY SMGEHPSTSD QDNSFKTDDF TFNYGWTYNK LDRGYFPTDG SRVNLTGKVT 

       610        620        630        640        650        660 
IPGSDNEYYK VTLDTATYVP IDDDHKWVVL GRTRWGYGDG LGGKEMPFYE NFYAGGSSTV 

       670        680        690        700        710        720 
RGFQSNTIGP KAVYFPHQAS NYDPDYDYEC ATQDGAKDLC KSDDAVGGNA MAVASLEFIT 

       730        740        750        760        770        780 
PTPFISDKYA NSVRTSFFWD MGTVWDTNWD SSQYSGYPDY SDPSNIRMSA GIALQWMSPL 

       790        800        810 
GPLVFSYAQP FKKYDGDKAE QFQFNIGKTW 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the Escherichia coli sigma E regulon."
Dartigalongue C., Missiakas D., Raina S.
J. Biol. Chem. 276:20866-20875(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[2]Allison H.E., Sergeant M.J., Cookson S.S., Yaxian Y., James C.E., Sharp R.J., Saunders J.R., McCarthy A.J.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[3]"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-32 AND 351-362.
Strain: K12 / EMG2.
[8]"Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli."
Wu T., Malinverni J., Ruiz N., Kim S., Silhavy T.J., Kahne D.
Cell 121:235-245(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, DISRUPTION PHENOTYPE.
Strain: K12.
[9]"Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant."
Doerrler W.T., Raetz C.R.H.
J. Biol. Chem. 280:27679-27687(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[11]"YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli."
Werner J., Misra R.
Mol. Microbiol. 57:1450-1459(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[12]"YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli."
Malinverni J.C., Werner J., Kim S., Sklar J.G., Kahne D., Misra R., Silhavy T.J.
Mol. Microbiol. 61:151-164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH BAMB AND BAMD.
Strain: K12.
[13]"Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli."
Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D., Silhavy T.J.
Proc. Natl. Acad. Sci. U.S.A. 104:6400-6405(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
Strain: K12.
[14]"Reconstitution of outer membrane protein assembly from purified components."
Hagan C.L., Kim S., Kahne D.
Science 328:890-892(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[15]"The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of beta-barrel assembly."
Hagan C.L., Kahne D.
Biochemistry 50:7444-7446(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[16]"Structural basis of outer membrane protein biogenesis in bacteria."
Albrecht R., Zeth K.
J. Biol. Chem. 286:27792-27803(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAMB AND BAMD.
[17]"Structure and function of an essential component of the outer membrane protein assembly machine."
Kim S., Malinverni J.C., Sliz P., Silhavy T.J., Harrison S.C., Kahne D.
Science 317:961-964(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 21-351, DOMAIN.
[18]"Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes."
Knowles T.J., Jeeves M., Bobat S., Dancea F., McClelland D., Palmer T., Overduin M., Henderson I.R.
Mol. Microbiol. 68:1216-1227(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 21-174, DOMAIN.
[19]"Crystal structure of YaeT: conformational flexibility and substrate recognition."
Gatzeva-Topalova P.Z., Walton T.A., Sousa M.C.
Structure 16:1873-1881(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 21-410, DOMAIN.
[20]"High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli."
Zhang H., Gao Z.Q., Hou H.F., Xu J.H., Li L.F., Su X.D., Dong Y.H.
Acta Crystallogr. F 67:734-738(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 266-420, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA64742.
RefSeqNP_414719.1. NC_000913.3.
YP_488479.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QCZX-ray2.70A/B21-351[»]
2QDFX-ray2.20A21-351[»]
2V9HNMR-A21-174[»]
3EFCX-ray3.30A21-410[»]
3Q6BX-ray1.50A266-420[»]
ProteinModelPortalP0A940.
SMRP0A940. Positions 23-810.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36019N.
IntActP0A940. 10 interactions.
STRING511145.b0177.

2D gel databases

SWISS-2DPAGEP0A940.

Proteomic databases

PaxDbP0A940.
PRIDEP0A940.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73288; AAC73288; b0177.
BAA77852; BAA77852; BAA77852.
GeneID12930510.
944870.
KEGGecj:Y75_p0173.
eco:b0177.
PATRIC32115465. VBIEscCol129921_0184.

Organism-specific databases

EchoBASEEB2541.
EcoGeneEG12676. bamA.

Phylogenomic databases

eggNOGCOG4775.
KOK07277.
OMAAMWRYLN.
OrthoDBEOG6F81K6.
PhylomeDBP0A940.
ProtClustDBPRK11067.

Enzyme and pathway databases

BioCycEcoCyc:G6093-MONOMER.
ECOL316407:JW0172-MONOMER.

Gene expression databases

GenevestigatorP0A940.

Family and domain databases

HAMAPMF_01430. OM_assembly_BamA.
InterProIPR000184. Bac_surfAg_D15.
IPR023707. OM_assembly_BamA.
IPR010827. Surface_Ag_variable_number.
[Graphical view]
PfamPF01103. Bac_surface_Ag. 1 hit.
PF07244. Surf_Ag_VNR. 5 hits.
[Graphical view]
PIRSFPIRSF006076. OM_assembly_OMP85. 1 hit.
TIGRFAMsTIGR03303. OM_YaeT. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A940.
PROP0A940.

Entry information

Entry nameBAMA_ECOLI
AccessionPrimary (citable) accession number: P0A940
Secondary accession number(s): P39170 expand/collapse secondary AC list , P39181, P77465, Q548B8, Q8KR94, Q9R2E3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene