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B5EFS0 (B5EFS0_GEOBB) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 33. Feed History...

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

Sequence length435 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

Transmembrane72 – 9221Helical; By similarity HAMAP-Rule MF_01465
Transmembrane117 – 13721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane151 – 17121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane180 – 20021Helical; By similarity HAMAP-Rule MF_01465
Transmembrane214 – 23421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane271 – 29121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane308 – 32821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane366 – 38621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane390 – 41021Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
B5EFS0 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: F777A2B99CC01FAA

FASTA43547,051
        10         20         30         40         50         60 
MIEAFQNIFK IPELKKKVLF SLAMLAVYRI GCHIPTPGID AQALAQFFKA AQGTLLGMFD 

        70         80         90        100        110        120 
MFSGGALEKL TVFALGIMPY ISSSIIFQLL TVVLPAVEKL SKEGDAGRKK IIQYTRYGTI 

       130        140        150        160        170        180 
VLAVVQAFGI SIGLEAMRGP AGELVVPNPG WGFRLMTVIT LTAGTAFIMW LGEQMSEKGI 

       190        200        210        220        230        240 
GNGISLIIFA GIVARIPTAI GNSFRLIKTG ELSLFVLLLI AAVMFAVIAA VVFMERGQRR 

       250        260        270        280        290        300 
IPIHYAKRVV GLKTVGAQSS HLPLKVNMAG VIPPIFASSI IMFPATVGNF IDVPWVQAAS 

       310        320        330        340        350        360 
KQLAPGKLLY EVLFVAFIVF FCYFYTAVTF NPVDVADNVK KQGGYVPGIR PGKETSDFLD 

       370        380        390        400        410        420 
AVLTKLTFAG AIYISAVCVL PSILIGKFNL PFYFGGTSLL IAVGVGMDTL SQIEAHLITR 

       430 
SYEGFMKGVR IQGRR

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References

[1]"Complete sequence of Geobacter bemidjiensis BEM."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Lovley D., Richardson P.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bem / ATCC BAA-1014 / DSM 16622.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001124 Genomic DNA. Translation: ACH37974.1.
RefSeqYP_002137770.1. NC_011146.1.

3D structure databases

ProteinModelPortalB5EFS0.
ModBaseSearch...

Protein-protein interaction databases

STRING404380.Gbem_0953.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH37974; ACH37974; Gbem_0953.
GeneID6783795.
KEGGgbm:Gbem_0953.
PATRIC21985616. VBIGeoBem56306_0955.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080586.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

Enzyme and pathway databases

BioCycGBEM404380:GHFR-969-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 nameB5EFS0_GEOBB
AccessionPrimary (citable) accession number: B5EFS0
Entry history
Integrated into UniProtKB/TrEMBL: October 14, 2008
Last sequence update: October 14, 2008
Last modified: May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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