Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein-export protein SecB

Gene

secB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

One of the proteins required for the normal export of some preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. Its substrates include AmpC, DegP, FhuA, FkpA, GBP, LamB, MalE (MBP), OmpA, OmpF, OmpT, OmpX, OppA, PhoE, TolB, TolC, YbgF, YcgK, YgiW and YncE.

GO - Molecular functioni

  1. unfolded protein binding Source: EcoCyc

GO - Biological processi

  1. protein folding Source: UniProtKB-HAMAP
  2. protein targeting Source: EcoliWiki
  3. protein tetramerization Source: EcoCyc
  4. protein transport Source: EcoliWiki
  5. protein transport by the Sec complex Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciEcoCyc:SECB.
ECOL316407:JW3584-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-export protein SecB
Gene namesi
Name:secB
Ordered Locus Names:b3609, JW3584
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10937. secB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Growth continues, but export of its substrates is blocked. Expression of chaperones DnaK, GroEL/ES, ClpB, and HslU increases.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 155155Protein-export protein SecBPRO_0000055370Add
BLAST

Proteomic databases

PaxDbiP0AG86.
PRIDEiP0AG86.

Expressioni

Gene expression databases

GenevestigatoriP0AG86.

Interactioni

Subunit structurei

Homotetramer, a dimer of dimers. One homotetramer interacts with 1 SecA dimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
secAP104084EBI-555877,EBI-543213

Protein-protein interaction databases

DIPiDIP-47924N.
IntActiP0AG86. 14 interactions.
MINTiMINT-1248893.
STRINGi511145.b3609.

Structurei

Secondary structure

1
155
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 2415Combined sources
Helixi28 – 314Combined sources
Beta strandi39 – 5214Combined sources
Beta strandi55 – 6814Combined sources
Beta strandi71 – 8818Combined sources
Helixi91 – 999Combined sources
Helixi101 – 12121Combined sources
Helixi133 – 1419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QYNX-ray2.35A/B/C/D1-153[»]
ProteinModelPortaliP0AG86.
SMRiP0AG86. Positions 9-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG86.

Family & Domainsi

Sequence similaritiesi

Belongs to the SecB family.Curated

Phylogenomic databases

eggNOGiCOG1952.
HOGENOMiHOG000218192.
InParanoidiP0AG86.
KOiK03071.
OMAiCPNVLFP.
OrthoDBiEOG6DVJZZ.
PhylomeDBiP0AG86.

Family and domain databases

Gene3Di3.10.420.10. 1 hit.
HAMAPiMF_00821. SecB.
InterProiIPR003708. SecB.
[Graphical view]
PfamiPF02556. SecB. 1 hit.
[Graphical view]
PRINTSiPR01594. SECBCHAPRONE.
SUPFAMiSSF54611. SSF54611. 1 hit.
TIGRFAMsiTIGR00809. secB. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AG86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ
60 70 80 90 100
LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA
110 120 130 140 150
YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE

EHQDA
Length:155
Mass (Da):17,277
Last modified:December 20, 2005 - v1
Checksum:i00514C5F393A643D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24489 Genomic DNA. Translation: AAA83907.1.
U00039 Genomic DNA. Translation: AAB18586.1.
U00096 Genomic DNA. Translation: AAC76633.1.
AP009048 Genomic DNA. Translation: BAE77683.1.
PIRiJS0126. VXECS.
RefSeqiNP_418066.1. NC_000913.3.
YP_491824.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76633; AAC76633; b3609.
BAE77683; BAE77683; BAE77683.
GeneIDi12932409.
948123.
KEGGiecj:Y75_p3565.
eco:b3609.
PATRICi32122703. VBIEscCol129921_3728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24489 Genomic DNA. Translation: AAA83907.1.
U00039 Genomic DNA. Translation: AAB18586.1.
U00096 Genomic DNA. Translation: AAC76633.1.
AP009048 Genomic DNA. Translation: BAE77683.1.
PIRiJS0126. VXECS.
RefSeqiNP_418066.1. NC_000913.3.
YP_491824.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QYNX-ray2.35A/B/C/D1-153[»]
ProteinModelPortaliP0AG86.
SMRiP0AG86. Positions 9-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47924N.
IntActiP0AG86. 14 interactions.
MINTiMINT-1248893.
STRINGi511145.b3609.

Proteomic databases

PaxDbiP0AG86.
PRIDEiP0AG86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76633; AAC76633; b3609.
BAE77683; BAE77683; BAE77683.
GeneIDi12932409.
948123.
KEGGiecj:Y75_p3565.
eco:b3609.
PATRICi32122703. VBIEscCol129921_3728.

Organism-specific databases

EchoBASEiEB0930.
EcoGeneiEG10937. secB.

Phylogenomic databases

eggNOGiCOG1952.
HOGENOMiHOG000218192.
InParanoidiP0AG86.
KOiK03071.
OMAiCPNVLFP.
OrthoDBiEOG6DVJZZ.
PhylomeDBiP0AG86.

Enzyme and pathway databases

BioCyciEcoCyc:SECB.
ECOL316407:JW3584-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AG86.
PROiP0AG86.

Gene expression databases

GenevestigatoriP0AG86.

Family and domain databases

Gene3Di3.10.420.10. 1 hit.
HAMAPiMF_00821. SecB.
InterProiIPR003708. SecB.
[Graphical view]
PfamiPF02556. SecB. 1 hit.
[Graphical view]
PRINTSiPR01594. SECBCHAPRONE.
SUPFAMiSSF54611. SSF54611. 1 hit.
TIGRFAMsiTIGR00809. secB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the Escherichia coli protein-export gene secB."
    Kumamoto C.A., Nault A.K.
    Gene 75:167-175(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  6. "Crystal structure of SecB from Escherichia coli."
    Dekker C., de Kruijff B., Gros P.
    J. Struct. Biol. 144:313-319(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
  7. "Defining the role of the Escherichia coli chaperone SecB using comparative proteomics."
    Baars L., Ytterberg A.J., Drew D., Wagner S., Thilo C., van Wijk K.J., de Gier J.W.
    J. Biol. Chem. 281:10024-10034(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATES, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100.
  8. "Bacterial protein secretion through the translocase nanomachine."
    Papanikou E., Karamanou S., Economou A.
    Nat. Rev. Microbiol. 5:839-851(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW OF PROTEIN SECRETION.

Entry informationi

Entry nameiSECB_ECOLI
AccessioniPrimary (citable) accession number: P0AG86
Secondary accession number(s): P15040, Q2M7S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 4, 2015
This is version 84 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.