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Protein

Protein translocase subunit SecY

Gene

secY

Organism
Staphylococcus aureus (strain MRSA252)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

GO - Biological processi

  1. intracellular protein transmembrane transport Source: UniProtKB-HAMAP
  2. protein targeting Source: UniProtKB-HAMAP
  3. protein transport by the Sec complex Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-2358-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecYUniRule annotation
Gene namesi
Name:secYUniRule annotation
Ordered Locus Names:SAR2315
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000596 Componenti: Chromosome

Subcellular locationi

Cell membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei18 – 3821HelicalUniRule annotationAdd
BLAST
Transmembranei68 – 8821HelicalUniRule annotationAdd
BLAST
Transmembranei117 – 13721HelicalUniRule annotationAdd
BLAST
Transmembranei147 – 16721HelicalUniRule annotationAdd
BLAST
Transmembranei179 – 19921HelicalUniRule annotationAdd
BLAST
Transmembranei217 – 23721HelicalUniRule annotationAdd
BLAST
Transmembranei269 – 28921HelicalUniRule annotationAdd
BLAST
Transmembranei308 – 32821HelicalUniRule annotationAdd
BLAST
Transmembranei368 – 38821HelicalUniRule annotationAdd
BLAST
Transmembranei389 – 40921HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. intracellular Source: GOC
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Protein translocase subunit SecYPRO_0000131743Add
BLAST

Interactioni

Subunit structurei

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.UniRule annotation

Protein-protein interaction databases

STRINGi282458.SAR2315.

Structurei

3D structure databases

ProteinModelPortaliQ6GEK3.
SMRiQ6GEK3. Positions 13-425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SecY/SEC61-alpha family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0201.
HOGENOMiHOG000080586.
KOiK03076.
OMAiQTYVISQ.
OrthoDBiEOG651SWP.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR030659. SecY_CS.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 1 hit.
TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
PROSITEiPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6GEK3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQTLVNFFR TKEVRNKIFF TLAMLVIFKI GTYIPAPGVN PAAFDNPQGS
60 70 80 90 100
QGATELLNTF GGGALKRFSI FAMGIVPYIT ASIVMQLLQM DIVPKFSEWA
110 120 130 140 150
KQGEVGRRKL NNVTRYLAIS LAFIQSIGMA FQFNNYLKGA LIINQSIMSY
160 170 180 190 200
LLIALVLTAG TAFLIWLGDQ ITQFGVGNGI SIIIFAGILS TLPASLIQFG
210 220 230 240 250
QTAFVGQEDT SLAWLKVLGL LVSLILLTVG AIYVLEAVRK IPIQYAKKQT
260 270 280 290 300
AQRLGSQATY LPLKVNSAGV IPVIFAMAFF LLPRTLTLFY PDKEWAQNIA
310 320 330 340 350
NAANPSSNVG MVVYIVLIIL FTYFYAFVQV NPEKMADNLK KQGSYVPGIR
360 370 380 390 400
PGEQTKKYIT KVLYRLTFVG SIFLAVISIL PILATKFMGL PQSIQIGGTS
410 420 430
LLIVIGVAIE TMKSLEAQVS QKEYKGFGGR
Length:430
Mass (Da):47,148
Last modified:July 18, 2004 - v1
Checksum:i31B735FEC788F1E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG41296.1.
RefSeqiYP_041670.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG41296; CAG41296; SAR2315.
KEGGisar:SAR2315.
PATRICi19548301. VBIStaAur71814_2327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG41296.1.
RefSeqiYP_041670.1. NC_002952.2.

3D structure databases

ProteinModelPortaliQ6GEK3.
SMRiQ6GEK3. Positions 13-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi282458.SAR2315.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG41296; CAG41296; SAR2315.
KEGGisar:SAR2315.
PATRICi19548301. VBIStaAur71814_2327.

Phylogenomic databases

eggNOGiCOG0201.
HOGENOMiHOG000080586.
KOiK03076.
OMAiQTYVISQ.
OrthoDBiEOG651SWP.

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-2358-MONOMER.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR030659. SecY_CS.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 1 hit.
TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
PROSITEiPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MRSA252.

Entry informationi

Entry nameiSECY_STAAR
AccessioniPrimary (citable) accession number: Q6GEK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2005
Last sequence update: July 18, 2004
Last modified: March 31, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.