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Protein

Outer membrane protein assembly factor BamB

Gene

bamB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 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. 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.UniRule annotation4 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

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

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14208. bamB.

Subcellular locationi

  • Cell outer membrane UniRule annotation1 Publication; Lipid-anchor UniRule annotation1 Publication

GO - Cellular componenti

  • Bam protein complex Source: EcoCyc
Complete GO annotation...

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.

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.UniRule annotation6 Publications

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 – 265Combined sources
Beta strandi45 – 506Combined sources
Turni53 – 586Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 755Combined sources
Beta strandi79 – 857Combined sources
Turni86 – 883Combined sources
Beta strandi91 – 966Combined sources
Beta strandi99 – 1057Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi129 – 1357Combined sources
Turni136 – 1383Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi169 – 1757Combined sources
Turni176 – 1783Combined sources
Beta strandi181 – 1866Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi206 – 2094Combined sources
Turni212 – 2143Combined sources
Beta strandi215 – 2206Combined sources
Turni221 – 2233Combined sources
Beta strandi226 – 2316Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi257 – 2615Combined sources
Beta strandi267 – 2715Combined sources
Turni272 – 2743Combined sources
Beta strandi277 – 2815Combined sources
Beta strandi286 – 2927Combined sources
Beta strandi295 – 3006Combined sources
Beta strandi305 – 3095Combined sources
Turni310 – 3123Combined sources
Beta strandi315 – 3195Combined sources
Turni321 – 3244Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi336 – 3405Combined sources
Beta strandi344 – 3507Combined sources
Turni351 – 3533Combined sources
Beta strandi356 – 3616Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi377 – 3815Combined sources
Beta strandi383 – 3853Combined sources
Beta strandi387 – 3915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4PK1X-ray3.10A21-392[»]
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.
InParanoidiP77774.
KOiK17713.
OMAiTAPALYN.
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

        10         20         30         40         50
MQLRKLLLPG LLSVTLLSGC SLFNSEEDVV KMSPLPTVEN QFTPTTAWST
60 70 80 90 100
SVGSGIGNFY SNLHPALADN VVYAADRAGL VKALNADDGK EIWSVSLAEK
110 120 130 140 150
DGWFSKEPAL LSGGVTVSGG HVYIGSEKAQ VYALNTSDGT VAWQTKVAGE
160 170 180 190 200
ALSRPVVSDG LVLIHTSNGQ LQALNEADGA VKWTVNLDMP SLSLRGESAP
210 220 230 240 250
TTAFGAAVVG GDNGRVSAVL MEQGQMIWQQ RISQATGSTE IDRLSDVDTT
260 270 280 290 300
PVVVNGVVFA LAYNGNLTAL DLRSGQIMWK RELGSVNDFI VDGNRIYLVD
310 320 330 340 350
QNDRVMALTI DGGVTLWTQS DLLHRLLTSP VLYNGNLVVG DSEGYLHWIN
360 370 380 390
VEDGRFVAQQ KVDSSGFQTE PVAADGKLLI QAKDGTVYSI TR
Length:392
Mass (Da):41,887
Last modified:February 1, 1997 - v1
Checksum:iBCFAFA061A486B31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75565.1.
AP009048 Genomic DNA. Translation: BAA16398.1.
PIRiG65027.
RefSeqiNP_417007.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC75565; AAC75565; b2512.
BAA16398; BAA16398; BAA16398.
GeneIDi946982.
KEGGiecj:Y75_p2465.
eco:b2512.
PATRICi32120417. VBIEscCol129921_2611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75565.1.
AP009048 Genomic DNA. Translation: BAA16398.1.
PIRiG65027.
RefSeqiNP_417007.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4PK1X-ray3.10A21-392[»]
ProteinModelPortaliP77774.
SMRiP77774. Positions 31-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

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

Proteomic databases

PaxDbiP77774.
PRIDEiP77774.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75565; AAC75565; b2512.
BAA16398; BAA16398; BAA16398.
GeneIDi946982.
KEGGiecj:Y75_p2465.
eco:b2512.
PATRICi32120417. VBIEscCol129921_2611.

Organism-specific databases

EchoBASEiEB3960.
EcoGeneiEG14208. bamB.

Phylogenomic databases

eggNOGiCOG1520.
HOGENOMiHOG000260994.
InParanoidiP77774.
KOiK17713.
OMAiTAPALYN.
OrthoDBiEOG6S7XRB.
PhylomeDBiP77774.

Enzyme and pathway databases

BioCyciEcoCyc:G7320-MONOMER.
ECOL316407:JW2496-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP77774.
PROiP77774.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 122 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.