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A0KF41 (A0KF41_AERHH) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 51. Feed History...

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

Sequence length442 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

Transmembrane23 – 4321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane76 – 9621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane121 – 14121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane151 – 17121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane184 – 20421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane214 – 23421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane271 – 29121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane316 – 33621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane374 – 39421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane396 – 41621Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
A0KF41 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 08FE224CA6855FE1

FASTA44248,266
        10         20         30         40         50         60 
MAKKPGLDVK AQGGLSELKS RLLFVLGAII VFRAGSYVPI PGIDAAVLAE LFQQQKGTII 

        70         80         90        100        110        120 
EMFNMFSGGA LSRASILALG IMPYISASII IQLLTVVHPA LAELKKEGES GRRKISQYTR 

       130        140        150        160        170        180 
WGTLVLGTFQ AIGIATGLPN MMQGLVTHPG LGFYFTAVVS LVTGTMFLMW LGEQITERGI 

       190        200        210        220        230        240 
GNGISLIIFT GIVAGLPHAI GATAEQARQG ELHILLLLLL GLIVFAVTYF VVFVERGQRR 

       250        260        270        280        290        300 
IVVNYAKRQQ GRQVFAAQST HLPLKVNMAG VIPAIFASSI ILFPGTITSW FGQGEGKIAD 

       310        320        330        340        350        360 
ILQQVSMVLQ PGQPLYEMLY AAAIIFFCFF YTALVFNPRE TADNLKKSGA FIPGIRPGEQ 

       370        380        390        400        410        420 
TARYIDKVMT RLTLAGALYI TFICLVPQFL MTAWNVQFYF GGTSLLIIVV VIMDFMAQVQ 

       430        440 
THMMSHQYGD VLRKANLKGY GR

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References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 7966 / NCIB 9240.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000462 Genomic DNA. Translation: ABK39412.1.
RefSeqYP_854863.1. NC_008570.1.

3D structure databases

ProteinModelPortalA0KF41.
ModBaseSearch...

Protein-protein interaction databases

STRING380703.AHA_0329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK39412; ABK39412; AHA_0329.
GeneID4489534.
KEGGaha:AHA_0329.
PATRIC20778136. VBIAerHyd135212_0318.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080585.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

Enzyme and pathway databases

BioCycAHYD380703:GH2M-470-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 nameA0KF41_AERHH
AccessionPrimary (citable) accession number: A0KF41
Entry history
Integrated into UniProtKB/TrEMBL: December 12, 2006
Last sequence update: December 12, 2006
Last modified: May 1, 2013
This is version 51 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