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Database: UniProt
Entry: Q5HH02
LinkDB: Q5HH02
Original site: Q5HH02 
ID   PTHP_STAAC              Reviewed;          88 AA.
AC   Q5HH02;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 76.
DE   RecName: Full=Phosphocarrier protein HPr;
DE            EC=2.7.11.-;
DE   AltName: Full=Histidine-containing protein;
GN   Name=ptsH; OrderedLocusNames=SACOL1091;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: General (non sugar-specific) component of the
CC       phosphoenolpyruvate-dependent sugar phosphotransferase system
CC       (sugar PTS). This major carbohydrate active-transport system
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane.
CC       The phosphoryl group from phosphoenolpyruvate (PEP) is transferred
CC       to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr
CC       then transfers it to the permease (enzymes II/III) (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: P-Ser-HPr interacts with the catabolite control protein
CC       A (CcpA), forming a complex that binds to DNA at the catabolite
CC       response elements cre, operator sites preceding a large number of
CC       catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in
CC       carbon catabolite repression (CCR), a mechanism that allows
CC       bacteria to coordinate and optimize the utilization of available
CC       carbon sources. P-Ser-HPr also plays a role in inducer exclusion,
CC       in which it probably interacts with several non-PTS permeases and
CC       inhibits their transport activity (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Protein HPr N(pi)-phospho-L-histidine +
CC       protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-
CC       histidine.
CC   -!- ENZYME REGULATION: Phosphorylation on Ser-46 inhibits the
CC       phosphoryl transfer from enzyme I to HPr. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 HPr domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00681}.
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DR   EMBL; CP000046; AAW37971.1; -; Genomic_DNA.
DR   RefSeq; YP_185955.1; NC_002951.2.
DR   ProteinModelPortal; Q5HH02; -.
DR   SMR; Q5HH02; 1-88.
DR   STRING; 93062.SACOL1091; -.
DR   EnsemblBacteria; AAW37971; AAW37971; SACOL1091.
DR   GeneID; 3237816; -.
DR   KEGG; sac:SACOL1091; -.
DR   PATRIC; 19528416; VBIStaAur112458_1061.
DR   eggNOG; COG1925; -.
DR   HOGENOM; HOG000278399; -.
DR   KO; K11189; -.
DR   OMA; TSESGIH; -.
DR   OrthoDB; EOG6XDGX2; -.
DR   BioCyc; SAUR93062:GCEP-1076-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1340.10; -; 1.
DR   InterPro; IPR000032; HPr_prot-like.
DR   InterPro; IPR001020; PTS_HPr_His_P_site.
DR   InterPro; IPR002114; PTS_HPr_Ser_P_site.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   PRINTS; PR00107; PHOSPHOCPHPR.
DR   SUPFAM; SSF55594; SSF55594; 1.
DR   TIGRFAMs; TIGR01003; PTS_HPr_family; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
DR   PROSITE; PS00369; PTS_HPR_HIS; 1.
DR   PROSITE; PS00589; PTS_HPR_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Kinase; Phosphoprotein;
KW   Phosphotransferase system; Serine/threonine-protein kinase;
KW   Sugar transport; Transcription; Transcription regulation; Transferase;
KW   Transport.
FT   CHAIN         1     88       Phosphocarrier protein HPr.
FT                                /FTId=PRO_0000107872.
FT   DOMAIN        1     88       HPr. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00681}.
FT   ACT_SITE     15     15       Pros-phosphohistidine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00681}.
FT   MOD_RES      46     46       Phosphoserine; by HPrK/P.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00681}.
SQ   SEQUENCE   88 AA;  9496 MW;  B2C6639D53226FF9 CRC64;
     MEQNSYVIID ETGIHARPAT MLVQTASKFD SDIQLEYNGK KVNLKSIMGV MSLGVGKDAE
     ITIYADGSDE SDAIQAISDV LSKEGLTK
//
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