Skip Header

Contribute Send feedback
Read comments (?) or add your own

B3PK57 (B3PK57_CELJU) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Protein translocase subunit SecY HAMAP-Rule MF_01465
Gene names
Name:secY HAMAP-Rule MF_01465
Ordered Locus Names:CJA_0719
OrganismCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP] EMBL ACE85795.1
Taxonomic identifier498211 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Cellvibrio ›

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently By similarity. HAMAP-Rule MF_01465

Subunit structure

Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA By similarity. HAMAP-Rule MF_01465

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01465.

Sequence similarities

Belongs to the SecY/SEC61-alpha family. RuleBase RU004349 HAMAP-Rule MF_01465

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Transmembrane24 – 4421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane76 – 9621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane122 – 14221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane149 – 16921Helical; By similarity HAMAP-Rule MF_01465
Transmembrane178 – 19821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane210 – 23021Helical; By similarity HAMAP-Rule MF_01465
Transmembrane269 – 28921Helical; By similarity HAMAP-Rule MF_01465
Transmembrane315 – 33521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane366 – 38621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane388 – 40821Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
B3PK57 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: A40D63D3B0D01484

FASTA44548,463
        10         20         30         40         50         60 
MATPSNLPLA NQRGLGELWA RLRFLFLAIV IYRIGTHIPV PGLDPERIAN LFNQNQGTIL 

        70         80         90        100        110        120 
GMFNMFSGGA LERMSILALG IMPYISASII MQLLTAVTPS LEQLKKEGDA GRRKINQYTR 

       130        140        150        160        170        180 
YFTVVLASVQ ALAMAVSFSG FAYGGEPGFA YYFIAVVSLV TGAIFMMWLG EQVTERGIGN 

       190        200        210        220        230        240 
GISMLIFAGI VAGMPSAIGQ AFESARQGDL NILALLIVAI LALVIIWLVV RIERGQRRIT 

       250        260        270        280        290        300 
VNYAKRQQGR QAYAAQSSHL PLKINMSGVI PAIFASSILL FPASIAQWFG QGGDGVINNV 

       310        320        330        340        350        360 
LQEIALAIGP GQPLYILLFA GLITFFCFFY TALMFNPREV ADNLKKSGAY IPGIRPGEHS 

       370        380        390        400        410        420 
AKYIDSVLTR LTVVGAIYMS AVCLLPEFLI VVTNVPFYLG GTSLLIVVVV LMDFMSQVQA 

       430        440 
HLMSHQYESL MKKSNLKGYG SGIVR

« Hide

References

[1]"Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ueda107.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000934 Genomic DNA. Translation: ACE85795.1.
RefSeqYP_001981228.1. NC_010995.1.

3D structure databases

ProteinModelPortalB3PK57.
ModBaseSearch...

Protein-protein interaction databases

STRING498211.CJA_0719.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE85795; ACE85795; CJA_0719.
GeneID6415973.
KEGGcja:CJA_0719.
PATRIC21324811. VBICelJap122165_0711.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080585.
KOK03076.
OMAFIMWLGE.
ProtClustDBCLSK2312913.

Enzyme and pathway databases

BioCycCJAP498211:GHIT-3174-MONOMER.

Family and domain databases

Gene3D1.10.3370.10. 1 hit.
HAMAPMF_01465. SecY.
InterProIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERPTHR10906. PTHR10906. 1 hit.
PfamPF00344. SecY. 1 hit.
[Graphical view]
PIRSFPIRSF004557. SecY. 1 hit.
SUPFAMSSF103491. SecY. 1 hit.
TIGRFAMsTIGR00967. 3a0501s007. 1 hit.
PROSITEPS00755. SECY_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB3PK57_CELJU
AccessionPrimary (citable) accession number: B3PK57
Entry history
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info