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A2RNN3 (A2RNN3_LACLM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 48. 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 RuleBase RU000537 HAMAP-Rule MF_01465
Gene names
Name:secY HAMAP-Rule MF_01465 EMBL CAL98924.1
Ordered Locus Names:llmg_2361
OrganismLactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP] EMBL CAL98924.1
Taxonomic identifier416870 [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. 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 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
A2RNN3 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 082A7639A05F04F3

FASTA43948,438
        10         20         30         40         50         60 
MFFKTLKEAF KVKDVRARIL FTIFILFVFR LGAHITAPGV 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

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References

[1]"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MG1363.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM406671 Genomic DNA. Translation: CAL98924.1.
RefSeqYP_001033604.1. NC_009004.1.

3D structure databases

ProteinModelPortalA2RNN3.
ModBaseSearch...

Protein-protein interaction databases

STRING416870.llmg_2361.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL98924; CAL98924; llmg_2361.
GeneID4797668.
KEGGllm:llmg_2361.
PATRIC22285932. VBILacLac4574_2404.

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.
PS00756. SECY_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA2RNN3_LACLM
AccessionPrimary (citable) accession number: A2RNN3
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2007
Last sequence update: March 6, 2007
Last modified: May 1, 2013
This is version 48 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