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Q6AD14 (Q6AD14_LEIXX) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 60. 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 AAT89730.1
Ordered Locus Names:Lxx20140
OrganismLeifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP] EMBL AAT89730.1
Taxonomic identifier281090 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Leifsonia ›

Protein attributes

Sequence length440 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

Transmembrane18 – 3821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane72 – 9221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane122 – 14221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane159 – 17921Helical; By similarity HAMAP-Rule MF_01465
Transmembrane191 – 21121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane217 – 23721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane271 – 29121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane319 – 33921Helical; By similarity HAMAP-Rule MF_01465
Transmembrane379 – 39921Helical; By similarity HAMAP-Rule MF_01465
Transmembrane400 – 42021Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
Q6AD14 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 5288D626BC4D2AC8

FASTA44048,220
        10         20         30         40         50         60 
MFSAVARIFR TPDLRRKIFF TLGIIALFRL GSFIPAPFVD FANVQTCLNA NQDTSGLYSL 

        70         80         90        100        110        120 
VNLFSGGALL KLSIFALGIM PYITASIIVQ LLRVVIPRFE TLYKEGQAGQ AKLTQYTRYL 

       130        140        150        160        170        180 
TIALGVLQST TLITVARSGA LFGTTAVSQC TQLITDDSWY AIMLMVITMT AGTGLIMWMG 

       190        200        210        220        230        240 
ELVTERGIGN GMSLLIFTSI AAQFPSSLWT IGQSQSIEIM LVVIAIGLLI VAAVVFVEQS 

       250        260        270        280        290        300 
QRRIPVQYAK RMVGRRTYGG NNTYIPIKVN MAGVVPVIFA SSLLYLPALI AQFNQPAAGK 

       310        320        330        340        350        360 
APAAWVTWIT NYLTKGDHPL YMLLYFLLIV GFTYFYVAIT FNPEEVADNM KKYGGFIPGI 

       370        380        390        400        410        420 
RAGRPTAEYL DYVLTRVTLP GSVYLGVIAL IPLVAFALLG ASQNFMFGGT SILIIVGVGL 

       430        440 
ETVKQIDSQL QQRHYEGLLR

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016822 Genomic DNA. Translation: AAT89730.1.
RefSeqYP_062835.1. NC_006087.1.

3D structure databases

ProteinModelPortalQ6AD14.
ModBaseSearch...

Protein-protein interaction databases

STRING281090.Lxx20140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT89730; AAT89730; Lxx20140.
GeneID2939414.
KEGGlxx:Lxx20140.
PATRIC22337708. VBILeiXyl11655_2091.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000080586.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

Enzyme and pathway databases

BioCycLXYL281090:GH0X-1907-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 nameQ6AD14_LEIXX
AccessionPrimary (citable) accession number: Q6AD14
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2004
Last sequence update: September 13, 2004
Last modified: May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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