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Q1JNZ7 (Q1JNZ7_STRPC) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 53. 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 namesRecommended name:
Protein translocase subunit SecY HAMAP-Rule MF_01465
Gene names
Name:secY HAMAP-Rule MF_01465 EMBL ABF31252.1
Ordered Locus Names:MGAS9429_Spy0064
OrganismStreptococcus pyogenes serotype M12 (strain MGAS9429) [Complete proteome] [HAMAP] EMBL ABF31252.1
Taxonomic identifier370551 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length450 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 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

Transmembrane35 – 5521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane84 – 10421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane132 – 15221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane167 – 18721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane195 – 21521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane232 – 25221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane285 – 30521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane326 – 34621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane384 – 40421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane410 – 43021Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
Q1JNZ7 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: B45D267BAEC07B15

FASTA45049,421
        10         20         30         40         50         60 
MLKVVQSKSS NEGILIMFLK ILKDALKIKT VRNKIFFTIF IILVFRIGTH ITVPGVNAKS 

        70         80         90        100        110        120 
LEQLSELPFL NMLNLVSGNA MRNFSVFSMG VSPYITASIV VQLLQMDILP KFVEWGKQGE 

       130        140        150        160        170        180 
VGRRKLNQAT RYISLVLAFA QSIGITAGFN TLSNVALVKT PDIKTYLLIG ALLTTGSVIV 

       190        200        210        220        230        240 
TWLGEQITDK GFGNGVSMII FAGIISSIPS AIATIREDYF VNVKASDLHS SYLIVGILII 

       250        260        270        280        290        300 
AVLAIVFFTT YVQQAEYKIP IQYTKLMQGA PTSSYLPLKV NPAGVIPVIF ASSITTIPST 

       310        320        330        340        350        360 
IIPFVQNGRD LPWLNRLQEI FNYQTPVGMI VYALLIILFS FFYTFVQVNP EKTAENLQKN 

       370        380        390        400        410        420 
SSYIPSVRPG RETEQFMSAL LKKLATVGAI FLAFISLAPI AAQQALNLSS SIALGGTSLL 

       430        440        450 
ILISTGIEGM KQLEGYLLKR KYVGFMNTAE

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References

[1]"Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus."
Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS9429.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000259 Genomic DNA. Translation: ABF31252.1.
RefSeqYP_595796.2. NC_008021.1.

3D structure databases

ProteinModelPortalQ1JNZ7.
ModBaseSearch...

Protein-protein interaction databases

STRING370551.MGAS9429_Spy0064.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF31252; ABF31252; MGAS9429_Spy0064.
GeneID4061517.
KEGGspk:MGAS9429_Spy0064.
PATRIC19751090. VBIStrPyo37061_0063.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080586.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

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 nameQ1JNZ7_STRPC
AccessionPrimary (citable) accession number: Q1JNZ7
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2006
Last sequence update: June 13, 2006
Last modified: May 1, 2013
This is version 53 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