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Protein

Outer membrane protein assembly factor BamE

Gene

bamE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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 that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD.UniRule annotation6 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein binding, bridging Source: EcoCyc

GO - Biological processi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10952-MONOMER.
ECOL316407:JW2598-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 BamEUniRule annotation
Gene namesi
Name:bamEUniRule annotation
Synonyms:smpA
Ordered Locus Names:b2617, JW2598
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10952. bamE.

Subcellular locationi

GO - Cellular componenti

  • integral component of cell outer membrane Source: EcoliWiki
  • membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutants show minor defects in the assembly of outer membrane proteins.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919UniRule annotationAdd
BLAST
Chaini20 – 11394Outer membrane protein assembly factor BamEPRO_0000032810Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP0A937.
PRIDEiP0A937.

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. Forms a subcomplex with BamC and BamD. Monomer in the periplasm, but is able to adopt a dimeric conformation in the cytoplasm.UniRule annotation7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself14EBI-6391574,EBI-6391574

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein binding, bridging Source: EcoCyc

Protein-protein interaction databases

BioGridi4259570. 130 interactions.
849957. 1 interaction.
DIPiDIP-10895N.
IntActiP0A937. 4 interactions.
MINTiMINT-8141263.
STRINGi511145.b2617.

Structurei

Secondary structure

1
113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 354Combined sources
Turni42 – 443Combined sources
Helixi52 – 598Combined sources
Beta strandi63 – 653Combined sources
Beta strandi68 – 703Combined sources
Beta strandi71 – 766Combined sources
Turni82 – 843Combined sources
Beta strandi85 – 873Combined sources
Beta strandi90 – 956Combined sources
Beta strandi99 – 1079Combined sources
Turni109 – 1124Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KM7NMR-A20-113[»]
2KXXNMR-A21-113[»]
2YH9X-ray1.80A/B/C34-113[»]
5AYWX-ray3.56E20-113[»]
5D0OX-ray2.90E1-113[»]
5D0QX-ray3.50E/I1-113[»]
5EKQX-ray3.39E20-113[»]
ProteinModelPortaliP0A937.
SMRiP0A937. Positions 21-113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A937.

Family & Domainsi

Sequence similaritiesi

Belongs to the BamE family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105YRI. Bacteria.
COG2913. LUCA.
HOGENOMiHOG000256181.
InParanoidiP0A937.
KOiK06186.
OMAiQPGHEKV.
OrthoDBiEOG6J48RK.
PhylomeDBiP0A937.

Family and domain databases

HAMAPiMF_00925. OM_assembly_BamE.
InterProiIPR026592. BamE.
IPR007450. Lipoprotein_SmpA/OmlA.
[Graphical view]
PfamiPF04355. SmpA_OmlA. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A937-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCKTLTAAA AVLLMLTAGC STLERVVYRP DINQGNYLTA NDVSKIRVGM
60 70 80 90 100
TQQQVAYALG TPLMSDPFGT NTWFYVFRQQ PGHEGVTQQT LTLTFNSSGV
110
LTNIDNKPAL SGN
Length:113
Mass (Da):12,302
Last modified:July 19, 2005 - v1
Checksum:iCFD8840C014AA0A2
GO

Sequence cautioni

The sequence CAA36847.1 differs from that shown.Sequence of unknown provenance, it does not match this entry.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36840 Genomic DNA. Translation: AAA79787.1.
U00096 Genomic DNA. Translation: AAC75666.2.
AP009048 Genomic DNA. Translation: BAA16502.1.
X52620 Genomic DNA. Translation: CAA36847.1. Sequence problems.
PIRiS11646.
T08630.
RefSeqiNP_417107.2. NC_000913.3.
WP_001203437.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75666; AAC75666; b2617.
BAA16502; BAA16502; BAA16502.
GeneIDi945583.
KEGGiecj:JW2598.
eco:b2617.
PATRICi32120633. VBIEscCol129921_2715.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36840 Genomic DNA. Translation: AAA79787.1.
U00096 Genomic DNA. Translation: AAC75666.2.
AP009048 Genomic DNA. Translation: BAA16502.1.
X52620 Genomic DNA. Translation: CAA36847.1. Sequence problems.
PIRiS11646.
T08630.
RefSeqiNP_417107.2. NC_000913.3.
WP_001203437.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KM7NMR-A20-113[»]
2KXXNMR-A21-113[»]
2YH9X-ray1.80A/B/C34-113[»]
5AYWX-ray3.56E20-113[»]
5D0OX-ray2.90E1-113[»]
5D0QX-ray3.50E/I1-113[»]
5EKQX-ray3.39E20-113[»]
ProteinModelPortaliP0A937.
SMRiP0A937. Positions 21-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259570. 130 interactions.
849957. 1 interaction.
DIPiDIP-10895N.
IntActiP0A937. 4 interactions.
MINTiMINT-8141263.
STRINGi511145.b2617.

Protein family/group databases

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

Proteomic databases

PaxDbiP0A937.
PRIDEiP0A937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75666; AAC75666; b2617.
BAA16502; BAA16502; BAA16502.
GeneIDi945583.
KEGGiecj:JW2598.
eco:b2617.
PATRICi32120633. VBIEscCol129921_2715.

Organism-specific databases

EchoBASEiEB0945.
EcoGeneiEG10952. bamE.

Phylogenomic databases

eggNOGiENOG4105YRI. Bacteria.
COG2913. LUCA.
HOGENOMiHOG000256181.
InParanoidiP0A937.
KOiK06186.
OMAiQPGHEKV.
OrthoDBiEOG6J48RK.
PhylomeDBiP0A937.

Enzyme and pathway databases

BioCyciEcoCyc:EG10952-MONOMER.
ECOL316407:JW2598-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A937.
PROiP0A937.

Family and domain databases

HAMAPiMF_00925. OM_assembly_BamE.
InterProiIPR026592. BamE.
IPR007450. Lipoprotein_SmpA/OmlA.
[Graphical view]
PfamiPF04355. SmpA_OmlA. 1 hit.
[Graphical view]
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. "Two new genes located between 2758 and 2761 kilobase pairs on the Escherichia coli genome."
    Chauhan A.K., Miczak A., Apirion D.
    J. Bacteriol. 173:3271-3272(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-113.
    Strain: K12.
  5. "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: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    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. "BamE modulates the Escherichia coli beta-barrel assembly machine component BamA."
    Rigel N.W., Schwalm J., Ricci D.P., Silhavy T.J.
    J. Bacteriol. 194:1002-1008(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  9. "Crystallization and preliminary X-ray data collection of the Escherichia coli lipoproteins BamC, BamD and BamE."
    Albrecht R., Zeth K.
    Acta Crystallogr. F 66:1586-1590(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, SUBUNIT.
  10. "Structural characterization of Escherichia coli BamE, a lipoprotein component of the beta-barrel assembly machinery complex."
    Kim K.H., Kang H.S., Okon M., Escobar-Cabrera E., McIntosh L.P., Paetzel M.
    Biochemistry 50:1081-1090(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 21-113, FUNCTION, SUBUNIT.
  11. Cited for: STRUCTURE BY NMR OF 21-113, SUBUNIT.
  12. "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 (1.8 ANGSTROMS) OF 34-113, SUBUNIT, FUNCTION.

Entry informationi

Entry nameiBAME_ECOLI
AccessioniPrimary (citable) accession number: P0A937
Secondary accession number(s): P23089
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: June 8, 2016
This is version 92 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

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 one 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.