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Q055C4 (Q055C4_LEPBL) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length460 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 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

Transmembrane18 – 3821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane62 – 8221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane118 – 13821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane160 – 18021Helical; By similarity HAMAP-Rule MF_01465
Transmembrane192 – 21221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane219 – 23921Helical; By similarity HAMAP-Rule MF_01465
Transmembrane276 – 29621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane324 – 34421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane384 – 40421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane412 – 43221Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
Q055C4 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 7D57E0A21D69B0A2

FASTA46050,881
        10         20         30         40         50         60 
MLTTFKNIFR IPELRQKIIF TLSMLLLFRM GTHITIPGIN PVVVAGIAND PSSEGLLGMV 

        70         80         90        100        110        120 
DLFAGGALLK FSIFALGIMP YISSSIVMQL FMVLVPSLQK LQKEGEEGRK KIGQYTKYGT 

       130        140        150        160        170        180 
VILCAIQSLA VIQLAKGWST GTELEPARYP GLINSSVVPY FYLIGILSIT TGTVLLIWLG 

       190        200        210        220        230        240 
EQITERGIGN GISLLIFAGI IGRLPESMVQ LFSTDTMDAL NVLILLILLI LLISLTVLLT 

       250        260        270        280        290        300 
QGVRKVPLQY GKQMVGRKMV QAKSQSIPFK VNGANVMPII FASSLILFPQ TIIQWLSSSS 

       310        320        330        340        350        360 
EQWAGWAIIM DFFNPFSQIW YHALFYYIIY TSLIIFFAYF YTAIQFNPAE LAENLKKYGG 

       370        380        390        400        410        420 
FIPGIRPGSH TKEYIEKVLN RITLPGAMFL AGLALAPYII IKFLDLSSNS GGGSLVYTFG 

       430        440        450        460 
GTSLLIMVGV ALETLKQIES QLLMRNYEGF MKKSKIKGRS

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References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L550 EMBL ABJ78071.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000348 Genomic DNA. Translation: ABJ78031.1.
CP000348 Genomic DNA. Translation: ABJ78071.1.
RefSeqYP_796964.1. NC_008508.1.
YP_797004.1. NC_008508.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING355276.LBL_0473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ78031; ABJ78031; LBL_0433.
ABJ78071; ABJ78071; LBL_0473.
GeneID4408865.
4408925.
KEGGlbl:LBL_0433.
lbl:LBL_0473.
PATRIC22364112. VBILepBor75619_0532.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080586.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

Enzyme and pathway databases

BioCycLBOR355276:GHUQ-732-MONOMER.
LBOR355276:GHUQ-772-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 nameQ055C4_LEPBL
AccessionPrimary (citable) accession number: Q055C4
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: May 1, 2013
This is version 56 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