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P77774

- BAMB_ECOLI

UniProt

P77774 - BAMB_ECOLI

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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

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

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: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
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.

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 – 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 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[»]
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.
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

        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.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P77774.
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

« 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: November 26, 2014
This is version 117 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