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Q68W98 (SECY_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein translocase subunit SecY
Gene names
Name:secY
Ordered Locus Names:RT0631
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length433 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.

Subcellular location

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

Sequence similarities

Belongs to the SecY/SEC61-alpha family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433Protein translocase subunit SecY HAMAP-Rule MF_01465
PRO_0000277282

Regions

Transmembrane17 – 3721Helical; Potential
Transmembrane71 – 9121Helical; Potential
Transmembrane117 – 13721Helical; Potential
Transmembrane141 – 16121Helical; Potential
Transmembrane184 – 20421Helical; Potential
Transmembrane212 – 23221Helical; Potential
Transmembrane268 – 28821Helical; Potential
Transmembrane310 – 33021Helical; Potential
Transmembrane366 – 38621Helical; Potential
Transmembrane388 – 40821Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q68W98 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 25E159B44F948454

FASTA43347,681
        10         20         30         40         50         60 
MGQNFSKKSS NDLVSRIIFT IFMLIICRIG SFIPIPGIDS IALNSVAEKN QFGILGMFNM 

        70         80         90        100        110        120 
LSGGSLGRMS IFALAIMPYI TASIIIQLMS VAYKPLENLK KEGESGKRKI NQLSRYLTVL 

       130        140        150        160        170        180 
LASFQAYGVA LSLESMVTNT GPVVILAGFF FRVTTVITLV VGTMLLMWLG EQITQRGIGN 

       190        200        210        220        230        240 
GTSLIIFIGI ISGVPSAIIS MFELSRKGAL SPLIAITVCI GVVLLIAIII FFEKAQRKLL 

       250        260        270        280        290        300 
VQYPKRQVGN KIYGGEATHM PLKLNTSGVI PPIFASSILL FPTTLANFSN SNSETMSMLS 

       310        320        330        340        350        360 
YYLGHGKPVY ILLYVVLIMF FSFFYTAIVF NSEETANNLR KYGAYIPGKR PGKNTSDYFD 

       370        380        390        400        410        420 
YILTRLTVIG GLYLSIICVI PELLMNKYVI SLSLGGTSFL IVVNVVLDTM TQIQTYLFSS 

       430 
KYEGLMKKIK LKN 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU04094.1.
RefSeqYP_067576.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68W98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257363.RT0631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU04094; AAU04094; RT0631.
GeneID2958744.
KEGGrty:RT0631.
PATRIC17910504. VBIRicTyp34752_0651.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080585.
KOK03076.
OMAISINIFY.
OrthoDBEOG651SWP.

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-662-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. SSF103491. 1 hit.
TIGRFAMsTIGR00967. 3a0501s007. 1 hit.
PROSITEPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSECY_RICTY
AccessionPrimary (citable) accession number: Q68W98
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 60 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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names