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B7NER6 (SECB_ECOLU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein-export protein secB
Gene names
Name:secB
Ordered Locus Names:ECUMN_4126
OrganismEscherichia coli O17:K52:H18 (strain UMN026 / ExPEC) [Complete proteome] [HAMAP]
Taxonomic identifier585056 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

One of the proteins required for the normal export of 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 By similarity. HAMAP MF_00821

Subunit structure

Homotetramer, a dimer of dimers. One homotetramer interacts with 1 secA dimer By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_00821.

Sequence similarities

Belongs to the secB family.

Ontologies

Keywords
   Biological processProtein transport
Translocation
Transport
   Cellular componentCytoplasm
   Molecular functionChaperone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein tetramerization

Inferred from electronic annotation. Source: InterPro

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionunfolded protein binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 155155Protein-export protein secB HAMAP MF_00821
PRO_1000195321

Sequences

Sequence LengthMass (Da)Tools
B7NER6 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 00514C5F393A643D

FASTA15517,277
        10         20         30         40         50         60 
MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL 

        70         80         90        100        110        120 
RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR 

       130        140        150 
GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU928163 Genomic DNA. Translation: CAR15267.1.
RefSeqYP_002414765.1. NC_011751.1.

3D structure databases

ProteinModelPortalB7NER6.
SMRB7NER6. Positions 9-144.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7NER6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000121119; EBESCP00000109607; EBESCG00000118462.
GeneID7156607.
GenomeReviewsGene locus ECUMN_4126 in contig CU928163_GR.
PATRIC18447565. VBIEscCol32010_4300.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010317.
OMAGFPPLMI.
ProtClustDBPRK05751.

Enzyme and pathway databases

BioCycECOL585056:ECUMN_4126-MONOMER.

Family and domain databases

HAMAPMF_00821. SecB.
[Tree]
InterProIPR003708. SecB.
[Graphical view]
Gene3DG3DSA:3.10.420.10. SecB. 1 hit.
PfamPF02556. SecB. 1 hit.
[Graphical view]
PRINTSPR01594. SECBCHAPRONE.
SUPFAMSSF54611. SecB. 1 hit.
TIGRFAMsTIGR00809. SecB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSECB_ECOLU
AccessionPrimary (citable) accession number: B7NER6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 24, 2009
Last modified: January 25, 2012
This is version 24 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