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Q02W45 (Q02W45_LACLS) 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 RuleBase RU000537
Gene names
Name:secY HAMAP-Rule MF_01465
Ordered Locus Names:LACR_2381 EMBL ABJ73827.1
OrganismLactococcus lactis subsp. cremoris (strain SK11) [Complete proteome] [HAMAP] EMBL ABJ73827.1
Taxonomic identifier272622 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Lactococcus ›

Protein attributes

Sequence length439 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 RuleBase RU000537

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.

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

Transmembrane19 – 3921Helical; By similarity HAMAP-Rule MF_01465
Transmembrane68 – 8821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane116 – 13621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane151 – 17121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane176 – 19621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane216 – 23621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane269 – 28921Helical; By similarity HAMAP-Rule MF_01465
Transmembrane312 – 33221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane373 – 39321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane396 – 41621Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
Q02W45 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: F8531196FDB235A4

FASTA43948,466
        10         20         30         40         50         60 
MFFKTLKEAF KVKDVRARIL FTIFILFVFR LGAHITVPGV NVQNLQQVAD LPFLSMMNLV 

        70         80         90        100        110        120 
SGNAMQNYSL FAMGVSPYIT ASIIVQLLQM DILPKFVEWS KQGEIGRRKL NQATRYITLV 

       130        140        150        160        170        180 
LAMAQSIGIT AGFQAMSSLN IVQNPNWQSY LMIGVLLTTG SMVVTWMGEQ INEKGFGSGV 

       190        200        210        220        230        240 
SVIIFAGIVS GIPSAIKSVY DEKFLNVRPS EIPMSWIFVI GLILSAIVII YVTTFVQQAE 

       250        260        270        280        290        300 
RKVPIQYTKL TQGAPTSSYL PLRVNPAGVI PVIFAGSITT APATILQFLQ RSQGSNVGWL 

       310        320        330        340        350        360 
STLQNALSYT TWTGMLFYAL LIVLFTFFYS FVQVNPEKMA ENLQKQGSYI PSVRPGKGTE 

       370        380        390        400        410        420 
KYVSRLLMRL ATVGSLFLGL ISIIPIAAQN VWGLPKIVAL GGTSLLILIQ VAIQAVKQLE 

       430 
GYLLKRKYAG FMDNPLETK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000425 Genomic DNA. Translation: ABJ73827.1.
RefSeqYP_811940.1. NC_008527.1.

3D structure databases

ProteinModelPortalQ02W45.
ModBaseSearch...

Protein-protein interaction databases

STRING272622.LACR_2381.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ73827; ABJ73827; LACR_2381.
GeneID4433737.
KEGGllc:LACR_2381.
PATRIC22291633. VBILacLac38071_2546.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080586.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

Enzyme and pathway databases

BioCycLLAC272622:GJUG-2381-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 nameQ02W45_LACLS
AccessionPrimary (citable) accession number: Q02W45
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 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)
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