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F0K7F5 (F0K7F5_CLOAE) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 18. 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 EMBL ADZ22155.1
Ordered Locus Names:CEA_G3118 EMBL ADZ22155.1
OrganismClostridium acetobutylicum (strain EA 2018) [Complete proteome] [HAMAP]
Taxonomic identifier863638 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length427 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
Transmembrane71 – 9121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane113 – 13321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane145 – 16521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane177 – 19721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane207 – 22721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane264 – 28421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane306 – 32621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane364 – 38421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane386 – 40621Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
F0K7F5 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 4E703F27D6ABCDB9

FASTA42747,097
        10         20         30         40         50         60 
MLSTLRNAWK VPELRKRMLF TIAMVLIFRM GNYIPVSGVD TSKILNLTNQ SGSLFGLYNM 

        70         80         90        100        110        120 
MTGGAFSQFS IFAMGVIPYI NASIIMQLLT VAIPSLEQLS KEGEEGRKKI QKITRYISVP 

       130        140        150        160        170        180 
LAALQSLTFY AVIRSAGAMQ TNSKLSVFLI ILTLTAASTF LMWLGDQITD KGIGNGASLI 

       190        200        210        220        230        240 
IFVNIISRFP STIYNIVKLQ SADTVNIVEI VVVAVIACVL FVGVVIASLA ERRIPVQYAG 

       250        260        270        280        290        300 
KAVGGKVARK QSSHIPINMN ASCIIAIIFA ISVMMFPTTI SQFWPTAKIT KFLTGSEYSP 

       310        320        330        340        350        360 
FKQNTIPYML LYLVLILFFT WFYTQITFKP EEMSENIHKS SGFIPGIRPG EPTTRFIERV 

       370        380        390        400        410        420 
LDKVSILGGL FASVIAIAPM IVEANGSFQG IHFASTGLLI VVGVALENLR IMQSQLTMRH 


YHGFLNE 

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References

[1]"Comparative genomic and transcriptomic analysis revealed genetic characteristics related to solvent formation and xylose utilization in Clostridium acetobutylicum EA 2018."
Hu S., Zheng H., Gu Y., Zhao J., Zhang W., Yang Y., Wang S., Zhao G., Yang S., Jiang W.
BMC Genomics 12:93-93(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EA 2018 EMBL ADZ22155.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002118 Genomic DNA. Translation: ADZ22155.1.
RefSeqYP_005672250.1. NC_017295.1.

3D structure databases

ProteinModelPortalF0K7F5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADZ22155; ADZ22155; CEA_G3118.
GeneID12233866.
KEGGcay:CEA_G3118.
PATRIC47113234. VBICloAce167171_3149.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK03076.
OMAFIMWLGE.

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 nameF0K7F5_CLOAE
AccessionPrimary (citable) accession number: F0K7F5
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: April 3, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)