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Q0I142 (Q0I142_HAES1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 55. Feed History...

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

Protein attributes

Sequence length441 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. RuleBase RU000537 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.

Membrane; Multi-pass membrane protein By similarity RuleBase RU003484.

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

Transmembrane24 – 4421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane75 – 9521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane127 – 14721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane152 – 17221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane181 – 20121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane215 – 23521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane272 – 29221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane313 – 33321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane373 – 39321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane398 – 41821Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
Q0I142 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 56FCF9DD74ADAB85

FASTA44148,387
        10         20         30         40         50         60 
MAKQPGYQNR STQSGTSELK SRLLFVLGAL IVFRIGSFIP VPGIDAAVLA QLLEQQKGTI 

        70         80         90        100        110        120 
IDMFNMFSGG ALSRASIFAL GIMPYISASI IIQLLTTVHP ALAELKKEGE AGRRKISKYT 

       130        140        150        160        170        180 
RYSTLALATI QAIGISTGLP NMLPGLVPNL GFSFYFTAVI SLVTGTMFLM WLGEQITERG 

       190        200        210        220        230        240 
IGNGISLIIF AGIVAGLPSA IGQTIEQARQ GQMHLLVLLL IAVIVFAVTY FVVFFERGQR 

       250        260        270        280        290        300 
RIKVEYAKRQ QGRQIVGGHS THLPLKVNMA GVIPAIFASS IILFPATLTS WFGQGSNLEW 

       310        320        330        340        350        360 
LTELSLLLHP GQPLYLIVYA VAIIFFSFFY TAMQYNPRDT ADNLKKSGAF IPGIRPGEQT 

       370        380        390        400        410        420 
SRYIDKIMTR LTLIGGLYIT FVCLVPYIMT SAWNVQFYFG GTSLLIVVVV IMDFIVQIQS 

       430        440 
HLMSTKYESA LKKANLKGFG Q 

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References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI24361.1.
RefSeqYP_718286.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I142.
ModBaseSearch...

Protein-protein interaction databases

STRING205914.HS_0080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI24361; ABI24361; HS_0080.
GeneID4239588.
KEGGhso:HS_0080.
PATRIC20280060. VBIHaeSom53361_0088.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080585.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-83-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.
PS00756. SECY_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ0I142_HAES1
AccessionPrimary (citable) accession number: Q0I142
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2006
Last sequence update: October 3, 2006
Last modified: May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)