Reviewed, UniProtKB/Swiss-Prot P0AG86 (SECB_ECOLI)

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) [Complete 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 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. HAMAP MF_00821
Subunit structure	Homotetramer, a dimer of dimers. One homotetramer interacts with 1 secA dimer. HAMAP MF_00821
Subcellular location	Cytoplasm HAMAP MF_00821.
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
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: HAMAP protein targeting Inferred from mutant phenotype. Source: UniProtKB protein tetramerization Inferred from electronic annotation. Source: InterPro protein transport by the Sec complex Inferred from mutant phenotype. Source: UniProtKB transmembrane transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 155

155

Protein-export protein secB HAMAP MF_00821

PRO_0000055370

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

155

Helix Strand Turn

Details...

Beta strand

10 – 24

15

Helix

28 – 31

4

Beta strand

39 – 52

14

Beta strand

55 – 68

14

Beta strand

71 – 88

18

Helix

91 – 99

9

Helix

101 – 121

21

Helix

133 – 141

9

Sequences

	Sequence		Length	Mass (Da)
	P0AG86-1 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 00514C5F393A643D	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

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: 2656409] [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: 8041620] [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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Crystal structure of SecB from Escherichia coli." Dekker C., de Kruijff B., Gros P. J. Struct. Biol. 144:313-319(2003) [PubMed: 14643199] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
[6]	"Bacterial protein secretion through the translocase nanomachine." Papanikou E., Karamanou S., Economou A. Nat. Rev. Microbiol. 5:839-851(2007) [PubMed: 17938627] [Abstract] Cited for: REVIEW OF PROTEIN SECRETION.

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

AP_004182.1.
NP_418066.1.

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0AG86.

PTM databases

PhosSite

P0AG86.

2-D gel databases

ECO2DBASE

A015.6. 6TH EDITION.

Genome annotation databases

GeneID

948123.

GenomeReviews

Gene locus JW3584 in contig AP009048_GR.
Gene locus b3609 in contig U00096_GR.

KEGG

ecj:JW3584.
eco:b3609.

Organism-specific databases

EchoBASE

EB0930.

EcoGene

EG10937. secB.

CMR

Search...

Phylogenomic databases

eggNOG

COG1952.

HOGENOM

HBG294212.

OMA

GFPPLMI.

Enzyme and pathway databases

BioCyc

EcoCyc:SECB.
ECOL168927:B3609-MONOMER.

Gene expression databases

Genevestigator

P0AG86.

Family and domain databases

HAMAP

MF_00821. SecB.
[Tree]

InterPro

IPR003708. SecB.
[Graphical view]

Gene3D

G3DSA:3.10.420.10. SecB. 1 hit.

Pfam

PF02556. SecB. 1 hit.
[Graphical view]

PRINTS

PR01594. SECBCHAPRONE.

TIGRFAMs

TIGR00809. secB. 1 hit.

ProtoNet

Search...

Other Resources

BindingDB

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:	February 9, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)