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P50829 (YPQE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative phosphotransferase enzyme IIA component YpqE
EC=2.7.1.-
Alternative name(s):
Putative PTS system EIIA component
Gene names
Name:ypqE
Ordered Locus Names:BSU22230
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane By similarity.

Subcellular location

Cytoplasm Potential.

Domain

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.

Sequence similarities

Contains 1 PTS EIIA type-1 domain.

Ontologies

Keywords
   Biological processPhosphotransferase system
Sugar transport
Transport
   Cellular componentCytoplasm
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionkinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

sugar:hydrogen symporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Putative phosphotransferase enzyme IIA component YpqE
PRO_0000186711

Regions

Domain36 – 140105PTS EIIA type-1

Sites

Active site881Tele-phosphohistidine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
P50829 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 7E3AC146345B0D17

FASTA16817,936
        10         20         30         40         50         60 
MLKKLFGMGK IQEKVTEEVI YSPADGTVMD LSDVPDPVFS QKMMGEGIAV EPSSGEIVSP 

        70         80         90        100        110        120 
AEGEVIQIFH TKHAVGIRTR SGIELLIHVG LETVNMNGEG FTAHIKEGDK VKVGDPLITC 

       130        140        150        160 
DLELIKEKAS STVIPIVIMN GEAVGSMVSA GEKAARKGES KLFTIKAK

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome."
Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P.
Microbiology 142:2005-2016(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L47838 Genomic DNA. Translation: AAB38467.1.
AL009126 Genomic DNA. Translation: CAB14140.1.
PIRH69940.
RefSeqNP_390105.1. NC_000964.3.

3D structure databases

ProteinModelPortalP50829.
SMRP50829. Positions 5-167.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU22230.

Proteomic databases

PaxDbP50829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14140; CAB14140; BSU22230.
GeneID939046.
KEGGbsu:BSU22230.
PATRIC18976255. VBIBacSub10457_2318.

Organism-specific databases

GenoListBSU22230.

Phylogenomic databases

eggNOGCOG2190.
HOGENOMHOG000224568.
KOK02777.
OMAPVFSEKM.
ProtClustDBCLSK887487.

Enzyme and pathway databases

BioCycBSUB:BSU22230-MONOMER.

Family and domain databases

InterProIPR011055. Dup_hybrid_motif.
IPR001127. PTS_EIIA_1_perm.
[Graphical view]
PfamPF00358. PTS_EIIA_1. 1 hit.
[Graphical view]
SUPFAMSSF51261. Dup_hybrid_motif. 1 hit.
TIGRFAMsTIGR00830. PTBA. 1 hit.
PROSITEPS51093. PTS_EIIA_TYPE_1. 1 hit.
PS00371. PTS_EIIA_TYPE_1_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameYPQE_BACSU
AccessionPrimary (citable) accession number: P50829
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents