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P0A940

- BAMA_ECOLI

UniProt

P0A940 - BAMA_ECOLI

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Protein

Outer membrane protein assembly factor BamA

Gene

bamA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 PublicationsUniRule annotation

GO - Biological processi

  1. Gram-negative-bacterium-type cell outer membrane assembly Source: EcoCyc
  2. protein insertion into membrane Source: EcoCyc
Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:G6093-MONOMER.
ECOL316407:JW0172-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12676. bamA.

Subcellular locationi

Cell outer membrane 1 PublicationUniRule annotation

GO - Cellular componenti

  1. Bam protein complex Source: EcoCyc
  2. cell outer membrane Source: EcoCyc
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Depletion results in the accumulation of incorrectly assembled outer membrane proteins, including TolC, OmpF, OmpC and OmpA. Deletion is lethal.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationUniRule annotationAdd
BLAST
Chaini21 – 810790Outer membrane protein assembly factor BamAPRO_0000033470Add
BLAST

Proteomic databases

PaxDbiP0A940.
PRIDEiP0A940.

2D gel databases

SWISS-2DPAGEP0A940.

Expressioni

Gene expression databases

GenevestigatoriP0A940.

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.7 PublicationsUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
bamBP7777416EBI-907371,EBI-907297
bamDP0AC0213EBI-907371,EBI-1128087

Protein-protein interaction databases

DIPiDIP-36019N.
IntActiP0A940. 10 interactions.
STRINGi511145.b0177.

Structurei

Secondary structure

1
810
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 336
Beta strandi35 – 373
Helixi39 – 446
Helixi56 – 6712
Beta strandi72 – 809
Beta strandi83 – 908
Beta strandi93 – 1019
Beta strandi103 – 1053
Helixi107 – 1159
Turni116 – 1183
Beta strandi121 – 1233
Helixi127 – 1293
Helixi130 – 14011
Helixi141 – 1444
Beta strandi146 – 1483
Beta strandi150 – 1589
Turni159 – 1613
Beta strandi162 – 1709
Beta strandi176 – 1849
Beta strandi186 – 1883
Helixi190 – 1945
Helixi195 – 1973
Turni210 – 2123
Helixi219 – 23113
Turni232 – 2343
Beta strandi239 – 2479
Beta strandi251 – 26111
Beta strandi267 – 27610
Helixi281 – 2877
Helixi298 – 31316
Turni314 – 3163
Beta strandi317 – 3193
Beta strandi321 – 3299
Turni330 – 3334
Beta strandi334 – 3429
Beta strandi348 – 3569
Beta strandi358 – 3603
Helixi362 – 3665
Beta strandi373 – 3764
Helixi379 – 39214
Beta strandi396 – 40510
Beta strandi408 – 41912
Beta strandi427 – 4337
Turni434 – 4363
Beta strandi437 – 45317
Beta strandi455 – 4628
Beta strandi464 – 47512
Turni479 – 4824
Beta strandi484 – 49512
Helixi496 – 4994
Beta strandi501 – 5033
Beta strandi505 – 52016
Beta strandi523 – 53715
Helixi543 – 5519
Beta strandi564 – 57916
Beta strandi584 – 5863
Beta strandi589 – 60012
Beta strandi604 – 6063
Beta strandi608 – 62013
Beta strandi622 – 6254
Beta strandi627 – 64317
Helixi648 – 6503
Beta strandi671 – 6766
Beta strandi685 – 6873
Beta strandi700 – 7056
Beta strandi708 – 72013
Helixi728 – 7325
Beta strandi733 – 74513
Turni751 – 7566
Beta strandi767 – 77812
Beta strandi781 – 79212
Beta strandi802 – 8098

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QCZX-ray2.70A/B21-351[»]
2QDFX-ray2.20A21-351[»]
2V9HNMR-A21-174[»]
3EFCX-ray3.30A21-410[»]
3Q6BX-ray1.50A266-420[»]
4C4VX-ray3.00A347-810[»]
B344-810[»]
4N75X-ray2.60A/B427-810[»]
ProteinModelPortaliP0A940.
SMRiP0A940. Positions 23-810.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A940.

Family & Domainsi

Domaini

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.4 Publications

Sequence similaritiesi

Belongs to the BamA family.UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiCOG4775.
InParanoidiP0A940.
KOiK07277.
OMAiFPVNENN.
OrthoDBiEOG6F81K6.
PhylomeDBiP0A940.

Family and domain databases

HAMAPiMF_01430. OM_assembly_BamA.
InterProiIPR000184. Bac_surfAg_D15.
IPR023707. OM_assembly_BamA.
IPR010827. Surface_Ag_variable_number.
[Graphical view]
PfamiPF01103. Bac_surface_Ag. 1 hit.
PF07244. Surf_Ag_VNR. 5 hits.
[Graphical view]
PIRSFiPIRSF006076. OM_assembly_OMP85. 1 hit.
TIGRFAMsiTIGR03303. OM_YaeT. 1 hit.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151E → Q in AAK64508. 1 PublicationCurated
Sequence conflicti228 – 2281S → I in AAK64508. 1 PublicationCurated
Sequence conflicti361 – 3611K → R in AAK64508. 1 PublicationCurated
Sequence conflicti632 – 6321R → C in AAK64508. 1 PublicationCurated
Sequence conflicti712 – 7121A → T in AAK64508. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_488479.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73288; AAC73288; b0177.
BAA77852; BAA77852; BAA77852.
GeneIDi12930510.
944870.
KEGGiecj:Y75_p0173.
eco:b0177.
PATRICi32115465. VBIEscCol129921_0184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A64742.
RefSeqi NP_414719.1. NC_000913.3.
YP_488479.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QCZ X-ray 2.70 A/B 21-351 [» ]
2QDF X-ray 2.20 A 21-351 [» ]
2V9H NMR - A 21-174 [» ]
3EFC X-ray 3.30 A 21-410 [» ]
3Q6B X-ray 1.50 A 266-420 [» ]
4C4V X-ray 3.00 A 347-810 [» ]
B 344-810 [» ]
4N75 X-ray 2.60 A/B 427-810 [» ]
ProteinModelPortali P0A940.
SMRi P0A940. Positions 23-810.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36019N.
IntActi P0A940. 10 interactions.
STRINGi 511145.b0177.

2D gel databases

SWISS-2DPAGE P0A940.

Proteomic databases

PaxDbi P0A940.
PRIDEi P0A940.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73288 ; AAC73288 ; b0177 .
BAA77852 ; BAA77852 ; BAA77852 .
GeneIDi 12930510.
944870.
KEGGi ecj:Y75_p0173.
eco:b0177.
PATRICi 32115465. VBIEscCol129921_0184.

Organism-specific databases

EchoBASEi EB2541.
EcoGenei EG12676. bamA.

Phylogenomic databases

eggNOGi COG4775.
InParanoidi P0A940.
KOi K07277.
OMAi FPVNENN.
OrthoDBi EOG6F81K6.
PhylomeDBi P0A940.

Enzyme and pathway databases

BioCyci EcoCyc:G6093-MONOMER.
ECOL316407:JW0172-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A940.
PROi P0A940.

Gene expression databases

Genevestigatori P0A940.

Family and domain databases

HAMAPi MF_01430. OM_assembly_BamA.
InterProi IPR000184. Bac_surfAg_D15.
IPR023707. OM_assembly_BamA.
IPR010827. Surface_Ag_variable_number.
[Graphical view ]
Pfami PF01103. Bac_surface_Ag. 1 hit.
PF07244. Surf_Ag_VNR. 5 hits.
[Graphical view ]
PIRSFi PIRSF006076. OM_assembly_OMP85. 1 hit.
TIGRFAMsi TIGR03303. OM_YaeT. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiBAMA_ECOLI
AccessioniPrimary (citable) accession number: P0A940
Secondary accession number(s): P39170
, P39181, P77465, Q548B8, Q8KR94, Q9R2E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [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

External Data

Dasty 3