Skip Header

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

A1VE96 (A1VE96_DESVV) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length418 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 inner 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

Transmembrane52 – 7221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane100 – 12021Helical; By similarity HAMAP-Rule MF_01465
Transmembrane138 – 15821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane163 – 18321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane197 – 21721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane251 – 27121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane293 – 31321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane349 – 36921Helical; By similarity HAMAP-Rule MF_01465
Transmembrane373 – 39321Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
A1VE96 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 145CB5F8EB2AF1D3

FASTA41845,389
        10         20         30         40         50         60 
MWTFLLLAAY RIGVHVPIPG VDSSALADFF ASVQNTLFGL FDMFSGGGLR NLSVFALGIM 

        70         80         90        100        110        120 
PYISASIILQ LLQVVSPDLK RLAKEEGAAG KRKLTQYTRY ATVLITVIQG LGIAIGLESM 

       130        140        150        160        170        180 
HSPAGAPVVL EAGWAFRLVT IITLTAGTVL IMWLGEQITE KGLGNGISLI IFSGIVAGIP 

       190        200        210        220        230        240 
GGILKSAQLI SAGDMSLFAA IVILALMGLV LAGIVFVERA QRRIPIHYAK RQVGRKMFGG 

       250        260        270        280        290        300 
QTTHLPLRVN TAGVIPPIFA SSLLLFPATV ANFATSDWLK SVASWFSPHT IPYNILFIAL 

       310        320        330        340        350        360 
IVFFSFFYTA IIFDPKDIAE NLKKGGGFIP GIRPGDKTKE YIDKVLTRIT LWGAIYISVI 

       370        380        390        400        410 
SVLPMFLIAQ FNVPFYFGGT SLLILVGVAM DFMSQIESHL ISRQYEGLMN KTRIKGQR 

« Hide

References

[1]"Contribution of mobile genetic elements to Desulfovibrio vulgaris genome plasticity."
Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S., He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P., Stahl D.A.
Environ. Microbiol. 11:2244-2252(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000527 Genomic DNA. Translation: ABM28762.1.
RefSeqYP_967189.2. NC_008751.1.

3D structure databases

ProteinModelPortalA1VE96.
ModBaseSearch...

Protein-protein interaction databases

STRING391774.Dvul_1745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM28762; ABM28762; Dvul_1745.
GeneID4663068.
KEGGdvl:Dvul_1745.
PATRIC21767366. VBIDesVul62463_1957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080586.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

Enzyme and pathway databases

BioCycDVUL391774:GHS0-1831-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 nameA1VE96_DESVV
AccessionPrimary (citable) accession number: A1VE96
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 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)