Skip Header

Contribute Send feedback
Read comments (?) or add your own

D5TMS3 (D5TMS3_BACT1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Protein translocase subunit SecY HAMAP-Rule MF_01465
Gene names
Name:secY HAMAP-Rule MF_01465 EMBL ADH07265.1
Ordered Locus Names:BMB171_C2453 EMBL ADH07265.1
OrganismBacillus thuringiensis (strain BMB171) [Complete proteome] [HAMAP] EMBL ADH07265.1
Taxonomic identifier714359 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length434 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

Transmembrane18 – 3821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane67 – 8721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane116 – 13621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane146 – 16621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane175 – 19521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane214 – 23421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane263 – 28321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane310 – 33021Helical; By similarity HAMAP-Rule MF_01465
Transmembrane370 – 39021Helical; By similarity HAMAP-Rule MF_01465
Transmembrane391 – 41121Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
D5TMS3 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: D6979912DB90AC9F

FASTA43447,719
        10         20         30         40         50         60 
MFRTISNFMR VAEIRRKILF TLAMLIVFRI GTFIPVPHTN AEVLKVQDQA NVLGMLNVFG 

        70         80         90        100        110        120 
GGALQHFSIF AVGITPYITA SIIVQLLQMD VIPKFSEWAK QGEMGRKKSA QFTRYFTIIL 

       130        140        150        160        170        180 
AFIQAIGMSY GFNNIAGGQL ITDQSWTTYL FIATVLTAGT AFLLWLGEQI TANGVGNGIS 

       190        200        210        220        230        240 
MIIFAGLVAA IPNVANQIYL QQFQNAGDQL FMHIIKIVLI GLVILAIVVG VIYIQQAVRK 

       250        260        270        280        290        300 
IPIQYAKAVS GNNQYQGAKN THLPLKVNSA GVIPVIFASA FLMTPRTIAQ LFPDSSVSKW 

       310        320        330        340        350        360 
LVANLDFAHP IGMTLYVGLI VAFTYFYAFI QVNPEQMAEN LKKQNGYVPG IRPGKATEQY 

       370        380        390        400        410        420 
VTKILYRLTF IGAIFLGAIS ILPLVFTKIA TLPPSAQIGG TSLLIIVGVA LETMKTLESQ 

       430 
LVKRHYKGFI KKVN

« Hide

References

[1]"Complete genome sequence of Bacillus thuringiensis mutant strain BMB171."
He J., Shao X., Zheng H., Li M., Wang J., Zhang Q., Li L., Liu Z., Sun M., Wang S., Yu Z.
J. Bacteriol. 192:4074-4075(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BMB171 EMBL ADH07265.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001903 Genomic DNA. Translation: ADH07265.1.
RefSeqYP_003664985.1. NC_014171.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADH07265; ADH07265; BMB171_C2453.
GeneID9193494.
KEGGbtb:BMB171_C2453.
PATRIC38131703. VBIBacThu148000_2636.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000080586.
KOK03076.

Enzyme and pathway databases

BioCycBTHU714359:GJBQ-2568-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 nameD5TMS3_BACT1
AccessionPrimary (citable) accession number: D5TMS3
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: May 1, 2013
This is version 21 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