Protein-export protein SecB - Escherichia coli (strain K12)

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P0AG86 (SECB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein-export protein SecB

Gene names

Name:	secB
Ordered Locus Names:	b3609, JW3584

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	155 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. HAMAP-Rule MF_00821
Subunit structure	Homotetramer, a dimer of dimers. One homotetramer interacts with 1 SecA dimer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00821.
Disruption phenotype	Growth continues, but export of its substrates is blocked. Expression of chaperones DnaK, GroEL/ES, ClpB, and HslU increases. Ref.7
Sequence similarities	Belongs to the SecB family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Cytoplasm
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: HAMAP protein targeting Inferred from mutant phenotype PubMed 6403503. Source: EcoliWiki protein tetramerization Inferred from electronic annotation. Source: InterPro protein transport by the Sec complex Inferred from mutant phenotype PubMed 6403503. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
secA	P10408	4	EBI-555877,EBI-543213

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 155

155

Protein-export protein SecB HAMAP-Rule MF_00821

PRO_0000055370

Secondary structure

155

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AG86 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 00514C5F393A643D
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FASTA

155

17,277

        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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M24489 Genomic DNA. Translation: AAA83907.1.
U00039 Genomic DNA. Translation: AAB18586.1.
U00096 Genomic DNA. Translation: AAC76633.1.
AP009048 Genomic DNA. Translation: BAE77683.1.

PIR

VXECS. JS0126.

RefSeq

NP_418066.1. NC_000913.2.
YP_491824.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QYN	X-ray	2.35	A/B/C/D	1-153	[»]

ProteinModelPortal

P0AG86.

SMR

P0AG86. Positions 9-144.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47924N.

IntAct

P0AG86. 14 interactions.

MINT

MINT-1248893.

STRING

511145.b3609.

PTM databases

PhosSite

P0810436.

Proteomic databases

PaxDb

P0AG86.

PRIDE

P0AG86.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76633; AAC76633; b3609.
BAE77683; BAE77683; BAE77683.

GeneID

12932409.
948123.

KEGG

ecj:Y75_p3565.
eco:b3609.

PATRIC

32122703. VBIEscCol129921_3728.

Organism-specific databases

EchoBASE

EB0930.

EcoGene

EG10937. secB.

Phylogenomic databases

eggNOG

COG1952.

HOGENOM

HOG000218192.

K03071.

OMA

GFPPLMI.

ProtClustDB

PRK05751.

Enzyme and pathway databases

BioCyc

EcoCyc:SECB.
ECOL316407:JW3584-MONOMER.

Gene expression databases

Genevestigator

P0AG86.

Family and domain databases

Gene3D

3.10.420.10. 1 hit.

HAMAP

MF_00821. SecB.

InterPro

IPR003708. SecB.
[Graphical view]

Pfam

PF02556. SecB. 1 hit.
[Graphical view]

PRINTS

PR01594. SECBCHAPRONE.

SUPFAM

SSF54611. SecB. 1 hit.

TIGRFAMs

TIGR00809. secB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0AG86.

Entry information

Entry name

SECB_ECOLI

Accession

Primary (citable) accession number: P0AG86
Secondary accession number(s): P15040, Q2M7S3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents