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A9MSX8 (A9MSX8_SALPB) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 41. Feed History...

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

Sequence length443 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

Transmembrane24 – 4421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane77 – 9721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane125 – 14521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane154 – 17421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane183 – 20321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane217 – 23721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane274 – 29421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane317 – 33721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane370 – 39021Helical; By similarity HAMAP-Rule MF_01465
Transmembrane397 – 41721Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
A9MSX8 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 311AF8453D412064

FASTA44348,530
        10         20         30         40         50         60 
MAKQPGLDFQ SAKGGLGELK RRLLFVIGAL IVFRIGSFIP IPGIDAAVLA KLLEQQRGTI 

        70         80         90        100        110        120 
IEMFNMFSGG ALSRASIFAL GIMPYISASI IIQLLTVVHP TLAEIKKEGE SGRRKISQYT 

       130        140        150        160        170        180 
RYGTLVLAIF QSIGIATGLP NMPGMQGLVM NPGFAFYFTA VVSLVTGTMF LMWLGEQITE 

       190        200        210        220        230        240 
RGIGNGISII IFAGIVAGLP PAIAHTIEQA RQGDLHFLVL LLVAVLVFAV TFFVVFVERG 

       250        260        270        280        290        300 
QRRIVVNYAK RQQGRRVYAA QSTHLPLKVN MAGVIPAIFA SSIILFPATI ASWFGGGTGW 

       310        320        330        340        350        360 
NWLTTISLYL QPGQPLYVLL YASAIIFFCF FYTALVFNPR ETADNLKKSG AFVPGIRPGE 

       370        380        390        400        410        420 
QTAKYIDKVM TRLTLVGALY ITFICLIPEF MRDAMKVPFY FGGTSLLIVV VVIMDFMAQV 

       430        440 
QTLMMSSQYE SALKKANLKG YGR

« Hide

References

[1]The Salmonella enterica serovar Paratyphi B Genome Sequencing Project
McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1250 / SPB7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000886 Genomic DNA. Translation: ABX69578.1.
RefSeqYP_001590411.1. NC_010102.1.

3D structure databases

ProteinModelPortalA9MSX8.
ModBaseSearch...

Protein-protein interaction databases

STRING272994.SPAB_04261.

Proteomic databases

PRIDEA9MSX8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX69578; ABX69578; SPAB_04261.
GeneID5779420.
KEGGspq:SPAB_04261.
PATRIC18535224. VBISalEnt120821_3442.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080585.
KOK03076.
OMAFIMWLGE.
ProtClustDBPRK09204.

Enzyme and pathway databases

BioCycSENT28901:GH9O-4250-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 nameA9MSX8_SALPB
AccessionPrimary (citable) accession number: A9MSX8
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: May 29, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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