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P77774

- BAMB_ECOLI

UniProt

P77774 - BAMB_ECOLI

Protein

Outer membrane protein assembly factor BamB

Gene

bamB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      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. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins.4 PublicationsUniRule annotation

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. 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:G7320-MONOMER.
    ECOL316407:JW2496-MONOMER.

    Protein family/group databases

    TCDBi1.B.33.1.3. the outer membrane protein insertion porin (bam complex) (ompip) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Outer membrane protein assembly factor BamBUniRule annotation
    Gene namesi
    Name:bamBUniRule annotation
    Synonyms:yfgL
    Ordered Locus Names:b2512, JW2496
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG14208. bamB.

    Subcellular locationi

    Cell outer membrane 1 PublicationUniRule annotation; Lipid-anchor 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. Bam protein complex Source: EcoCyc

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919UniRule annotationAdd
    BLAST
    Chaini20 – 392373Outer membrane protein assembly factor BamBPRO_0000042211Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi20 – 201N-palmitoyl cysteineCurated
    Lipidationi20 – 201S-diacylglycerol cysteineCurated

    Keywords - PTMi

    Lipoprotein, Palmitate

    Proteomic databases

    PaxDbiP77774.
    PRIDEiP77774.

    Expressioni

    Gene expression databases

    GenevestigatoriP77774.

    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. Monomer. Interacts directly with BamA.6 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-907297,EBI-907297
    bamAP0A94016EBI-907297,EBI-907371
    surAP0ABZ62EBI-907297,EBI-558651

    Protein-protein interaction databases

    DIPiDIP-12042N.
    IntActiP77774. 8 interactions.
    STRINGi511145.b2512.

    Structurei

    Secondary structure

    1
    392
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 265
    Beta strandi45 – 506
    Turni53 – 586
    Beta strandi66 – 683
    Beta strandi71 – 755
    Beta strandi79 – 857
    Turni86 – 883
    Beta strandi91 – 966
    Beta strandi99 – 1057
    Beta strandi111 – 1188
    Beta strandi121 – 1266
    Beta strandi129 – 1357
    Turni136 – 1383
    Beta strandi141 – 1466
    Beta strandi156 – 1583
    Beta strandi161 – 1655
    Beta strandi169 – 1757
    Turni176 – 1783
    Beta strandi181 – 1866
    Beta strandi201 – 2033
    Beta strandi206 – 2094
    Turni212 – 2143
    Beta strandi215 – 2206
    Turni221 – 2233
    Beta strandi226 – 2316
    Beta strandi252 – 2543
    Beta strandi257 – 2615
    Beta strandi267 – 2715
    Turni272 – 2743
    Beta strandi277 – 2815
    Beta strandi286 – 2927
    Beta strandi295 – 3006
    Beta strandi305 – 3095
    Turni310 – 3123
    Beta strandi315 – 3195
    Turni321 – 3244
    Beta strandi331 – 3333
    Beta strandi336 – 3405
    Beta strandi344 – 3507
    Turni351 – 3533
    Beta strandi356 – 3616
    Beta strandi372 – 3743
    Beta strandi377 – 3815
    Beta strandi383 – 3853
    Beta strandi387 – 3915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YH3X-ray2.60A22-392[»]
    2YMSX-ray2.10A62-191[»]
    B113-186[»]
    C248-322[»]
    D247-320[»]
    3P1LX-ray2.60A21-392[»]
    3PRWX-ray1.80A21-392[»]
    3Q7MX-ray1.65A21-392[»]
    3Q7NX-ray1.77A21-392[»]
    3Q7OX-ray2.09A21-392[»]
    ProteinModelPortaliP77774.
    SMRiP77774. Positions 31-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP77774.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the BamB family.UniRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1520.
    HOGENOMiHOG000260994.
    KOiK17713.
    OMAiSNLHPAW.
    OrthoDBiEOG6S7XRB.
    PhylomeDBiP77774.

    Family and domain databases

    Gene3Di2.140.10.10. 1 hit.
    HAMAPiMF_00923. OM_assembly_BamB.
    InterProiIPR017687. BamB.
    IPR018391. PQQ_beta_propeller_repeat.
    IPR002372. PQQ_repeat.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    [Graphical view]
    PfamiPF01011. PQQ. 3 hits.
    [Graphical view]
    SMARTiSM00564. PQQ. 7 hits.
    [Graphical view]
    SUPFAMiSSF50998. SSF50998. 1 hit.
    TIGRFAMsiTIGR03300. assembly_YfgL. 1 hit.
    PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P77774-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLRKLLLPG LLSVTLLSGC SLFNSEEDVV KMSPLPTVEN QFTPTTAWST    50
    SVGSGIGNFY SNLHPALADN VVYAADRAGL VKALNADDGK EIWSVSLAEK 100
    DGWFSKEPAL LSGGVTVSGG HVYIGSEKAQ VYALNTSDGT VAWQTKVAGE 150
    ALSRPVVSDG LVLIHTSNGQ LQALNEADGA VKWTVNLDMP SLSLRGESAP 200
    TTAFGAAVVG GDNGRVSAVL MEQGQMIWQQ RISQATGSTE IDRLSDVDTT 250
    PVVVNGVVFA LAYNGNLTAL DLRSGQIMWK RELGSVNDFI VDGNRIYLVD 300
    QNDRVMALTI DGGVTLWTQS DLLHRLLTSP VLYNGNLVVG DSEGYLHWIN 350
    VEDGRFVAQQ KVDSSGFQTE PVAADGKLLI QAKDGTVYSI TR 392
    Length:392
    Mass (Da):41,887
    Last modified:February 1, 1997 - v1
    Checksum:iBCFAFA061A486B31
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75565.1.
    AP009048 Genomic DNA. Translation: BAA16398.1.
    PIRiG65027.
    RefSeqiNP_417007.1. NC_000913.3.
    YP_490740.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75565; AAC75565; b2512.
    BAA16398; BAA16398; BAA16398.
    GeneIDi12931593.
    946982.
    KEGGiecj:Y75_p2465.
    eco:b2512.
    PATRICi32120417. VBIEscCol129921_2611.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75565.1 .
    AP009048 Genomic DNA. Translation: BAA16398.1 .
    PIRi G65027.
    RefSeqi NP_417007.1. NC_000913.3.
    YP_490740.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YH3 X-ray 2.60 A 22-392 [» ]
    2YMS X-ray 2.10 A 62-191 [» ]
    B 113-186 [» ]
    C 248-322 [» ]
    D 247-320 [» ]
    3P1L X-ray 2.60 A 21-392 [» ]
    3PRW X-ray 1.80 A 21-392 [» ]
    3Q7M X-ray 1.65 A 21-392 [» ]
    3Q7N X-ray 1.77 A 21-392 [» ]
    3Q7O X-ray 2.09 A 21-392 [» ]
    ProteinModelPortali P77774.
    SMRi P77774. Positions 31-391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-12042N.
    IntActi P77774. 8 interactions.
    STRINGi 511145.b2512.

    Protein family/group databases

    TCDBi 1.B.33.1.3. the outer membrane protein insertion porin (bam complex) (ompip) family.

    Proteomic databases

    PaxDbi P77774.
    PRIDEi P77774.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75565 ; AAC75565 ; b2512 .
    BAA16398 ; BAA16398 ; BAA16398 .
    GeneIDi 12931593.
    946982.
    KEGGi ecj:Y75_p2465.
    eco:b2512.
    PATRICi 32120417. VBIEscCol129921_2611.

    Organism-specific databases

    EchoBASEi EB3960.
    EcoGenei EG14208. bamB.

    Phylogenomic databases

    eggNOGi COG1520.
    HOGENOMi HOG000260994.
    KOi K17713.
    OMAi SNLHPAW.
    OrthoDBi EOG6S7XRB.
    PhylomeDBi P77774.

    Enzyme and pathway databases

    BioCyci EcoCyc:G7320-MONOMER.
    ECOL316407:JW2496-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P77774.
    PROi P77774.

    Gene expression databases

    Genevestigatori P77774.

    Family and domain databases

    Gene3Di 2.140.10.10. 1 hit.
    HAMAPi MF_00923. OM_assembly_BamB.
    InterProi IPR017687. BamB.
    IPR018391. PQQ_beta_propeller_repeat.
    IPR002372. PQQ_repeat.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    [Graphical view ]
    Pfami PF01011. PQQ. 3 hits.
    [Graphical view ]
    SMARTi SM00564. PQQ. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 1 hit.
    TIGRFAMsi TIGR03300. assembly_YfgL. 1 hit.
    PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "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, SUBCELLULAR LOCATION.
      Strain: K12.
    5. "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: SUBUNIT, INTERACTION WITH BAMA.
      Strain: K12.
    6. "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.
    7. "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.
    8. "Augmenting beta-augmentation: Structural basis of how BamB binds BamA and may support folding of outer membrane proteins."
      Heuck A., Schleiffer A., Clausen T.
      Submitted (NOV-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 21-392.
    9. "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: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 22-392, INTERACTION WITH BAMA, SUBUNIT, FUNCTION.
    10. "Crystal structure of Escherichia coli BamB, a lipoprotein component of the beta-barrel assembly machinery complex."
      Kim K.H., Paetzel M.
      J. Mol. Biol. 406:667-678(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 21-392.
    11. "The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex."
      Noinaj N., Fairman J.W., Buchanan S.K.
      J. Mol. Biol. 407:248-260(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 21-392, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiBAMB_ECOLI
    AccessioniPrimary (citable) accession number: P77774
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 115 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, 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