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P0A940

- BAMA_ECOLI

UniProt

P0A940 - BAMA_ECOLI

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
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    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 - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

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

    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

    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.
    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

    MAMKKLLIAS LLFSSATVYG AEGFVVKDIH FEGLQRVAVG AALLSMPVRT    50
    GDTVNDEDIS NTIRALFATG NFEDVRVLRD GDTLLVQVKE RPTIASITFS 100
    GNKSVKDDML KQNLEASGVR VGESLDRTTI ADIEKGLEDF YYSVGKYSAS 150
    VKAVVTPLPR NRVDLKLVFQ EGVSAEIQQI NIVGNHAFTT DELISHFQLR 200
    DEVPWWNVVG DRKYQKQKLA GDLETLRSYY LDRGYARFNI DSTQVSLTPD 250
    KKGIYVTVNI TEGDQYKLSG VEVSGNLAGH SAEIEQLTKI EPGELYNGTK 300
    VTKMEDDIKK LLGRYGYAYP RVQSMPEIND ADKTVKLRVN VDAGNRFYVR 350
    KIRFEGNDTS KDAVLRREMR QMEGAWLGSD LVDQGKERLN RLGFFETVDT 400
    DTQRVPGSPD QVDVVYKVKE RNTGSFNFGI GYGTESGVSF QAGVQQDNWL 450
    GTGYAVGING TKNDYQTYAE LSVTNPYFTV DGVSLGGRLF YNDFQADDAD 500
    LSDYTNKSYG TDVTLGFPIN EYNSLRAGLG YVHNSLSNMQ PQVAMWRYLY 550
    SMGEHPSTSD QDNSFKTDDF TFNYGWTYNK LDRGYFPTDG SRVNLTGKVT 600
    IPGSDNEYYK VTLDTATYVP IDDDHKWVVL GRTRWGYGDG LGGKEMPFYE 650
    NFYAGGSSTV RGFQSNTIGP KAVYFPHQAS NYDPDYDYEC ATQDGAKDLC 700
    KSDDAVGGNA MAVASLEFIT PTPFISDKYA NSVRTSFFWD MGTVWDTNWD 750
    SSQYSGYPDY SDPSNIRMSA GIALQWMSPL GPLVFSYAQP FKKYDGDKAE 800
    QFQFNIGKTW 810
    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.
    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

    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 1, 2014
    This is version 88 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