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Q8A496 (Q8A496_BACTN) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length447 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. HAMAP-Rule MF_01465 RuleBase RU004349

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Transmembrane21 – 4121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane75 – 9521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane121 – 14121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane153 – 17321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane181 – 20121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane217 – 23721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane272 – 29221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane312 – 33221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane373 – 39321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane394 – 41421Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
Q8A496 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 18CDE8CE1882CB5F

FASTA44749,219
        10         20         30         40         50         60 
MRKAIETLKN IWKIEDLRQR ILITILFVAI YRFGSYVVLP GINPAMLAKL HEQTSEGLLA 

        70         80         90        100        110        120 
LLNMFSGGAF SNASIFALGI MPYISASIVI QLLGIAVPYF QKLQREGESG RRKMNQYTRY 

       130        140        150        160        170        180 
LTIAILLVQA PSYLLNLKMQ AGPSLNASLD WTLFMVTSTI ILAAGSMFIL WLGERITDKG 

       190        200        210        220        230        240 
IGNGISFIIL IGIIARFPDA LIQEVVSRVA NKSGGLIMFI IEVVFLLLVI GAAILLVQGT 

       250        260        270        280        290        300 
RKIPVQYAKR IVGNKQYGGA RQYIPLKVNA AGVMPIIFAQ AIMFIPITFI GFSNNVNNAG 

       310        320        330        340        350        360 
GFLHAFTDHT SFWYNFVFAV MIILFTYFYT AITINPTQMA EDMKRNNGFI PGIKPGKKTA 

       370        380        390        400        410        420 
EYIDDIMSRI TLPGSFFLAL VAIMPAFAGI FGVQAGFAQF FGGTSLLILV GVVLDTLQQV 

       430        440 
ESHLLMRHYD GLLKSGRIKG RAGVAAY

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References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015928 Genomic DNA. Translation: AAO77813.1.
RefSeqNP_811619.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ8A496.
ModBaseSearch...

Protein-protein interaction databases

STRING226186.BT_2707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO77813; AAO77813; BT_2707.
GeneID1072446.
KEGGbth:BT_2707.
PATRIC21060357. VBIBacThe70966_2750.

Phylogenomic databases

HOGENOMHOG000080586.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-2761-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 nameQ8A496_BACTN
AccessionPrimary (citable) accession number: Q8A496
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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