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P77774 (BAMB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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 BamB
Gene names
Name:bamB
Synonyms:yfgL
Ordered Locus Names:b2512, JW2496
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length392 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. 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. Ref.6 Ref.7 Ref.9 Ref.11

Subunit structure

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.11

Subcellular location

Cell outer membrane; Lipid-anchor Ref.4.

Sequence similarities

Belongs to the BamB family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 392373Outer membrane protein assembly factor BamB HAMAP-Rule MF_00923
PRO_0000042211

Amino acid modifications

Lipidation201N-palmitoyl cysteine Probable
Lipidation201S-diacylglycerol cysteine Probable

Secondary structure

................................................................................... 392
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P77774 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: BCFAFA061A486B31

FASTA39241,887
        10         20         30         40         50         60 
MQLRKLLLPG LLSVTLLSGC SLFNSEEDVV KMSPLPTVEN QFTPTTAWST SVGSGIGNFY 

        70         80         90        100        110        120 
SNLHPALADN VVYAADRAGL VKALNADDGK EIWSVSLAEK DGWFSKEPAL LSGGVTVSGG 

       130        140        150        160        170        180 
HVYIGSEKAQ VYALNTSDGT VAWQTKVAGE ALSRPVVSDG LVLIHTSNGQ LQALNEADGA 

       190        200        210        220        230        240 
VKWTVNLDMP SLSLRGESAP TTAFGAAVVG GDNGRVSAVL MEQGQMIWQQ RISQATGSTE 

       250        260        270        280        290        300 
IDRLSDVDTT PVVVNGVVFA LAYNGNLTAL DLRSGQIMWK RELGSVNDFI VDGNRIYLVD 

       310        320        330        340        350        360 
QNDRVMALTI DGGVTLWTQS DLLHRLLTSP VLYNGNLVVG DSEGYLHWIN VEDGRFVAQQ 

       370        380        390 
KVDSSGFQTE PVAADGKLLI QAKDGTVYSI TR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC75565.1.
AP009048 Genomic DNA. Translation: BAA16398.1.
PIRG65027.
RefSeqNP_417007.1. NC_000913.3.
YP_490740.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP77774.
SMRP77774. Positions 31-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP77774. 8 interactions.
STRING511145.b2512.

Protein family/group databases

TCDB1.B.33.1.3. the outer membrane protein insertion porin (bam complex) (ompip) family.

Proteomic databases

PaxDbP77774.
PRIDEP77774.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75565; AAC75565; b2512.
BAA16398; BAA16398; BAA16398.
GeneID12931593.
946982.
KEGGecj:Y75_p2465.
eco:b2512.
PATRIC32120417. VBIEscCol129921_2611.

Organism-specific databases

EchoBASEEB3960.
EcoGeneEG14208. bamB.

Phylogenomic databases

eggNOGCOG1520.
HOGENOMHOG000260994.
KOK17713.
OMASNLHPAW.
OrthoDBEOG6S7XRB.
PhylomeDBP77774.
ProtClustDBPRK11138.

Enzyme and pathway databases

BioCycEcoCyc:G7320-MONOMER.
ECOL316407:JW2496-MONOMER.

Gene expression databases

GenevestigatorP77774.

Family and domain databases

Gene3D2.140.10.10. 1 hit.
HAMAPMF_00923. OM_assembly_BamB.
InterProIPR017687. BamB.
IPR018391. PQQ_beta_propeller_repeat.
IPR002372. PQQ_repeat.
IPR027295. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
[Graphical view]
PfamPF01011. PQQ. 3 hits.
[Graphical view]
SMARTSM00564. PQQ. 7 hits.
[Graphical view]
SUPFAMSSF50998. SSF50998. 1 hit.
TIGRFAMsTIGR03300. assembly_YfgL. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP77774.
PROP77774.

Entry information

Entry nameBAMB_ECOLI
AccessionPrimary (citable) accession number: P77774
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 112 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