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Database: UniProt
Entry: P0A0E3
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Original site: P0A0E3 
ID   PTHP_STAAU              Reviewed;          88 AA.
AC   P0A0E3; P02907;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   16-APR-2014, entry version 54.
DE   RecName: Full=Phosphocarrier protein HPr;
DE            EC=2.7.11.-;
DE   AltName: Full=Histidine-containing protein;
GN   Name=ptsH;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=305A;
RA   Kravanja M., Engelmann R., Christiansen I., Hengstenberg W.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE.
RX   PubMed=862621; DOI=10.1111/j.1432-1033.1977.tb11527.x;
RA   Beyreuther K., Raufuss H., Schrecker O., Hengstenberg W.;
RT   "The phosphoenolpyruvate-dependent phosphotransferase system of
RT   Staphylococcus aureus. 1. Amino-acid sequence of the phosphocarrier
RT   protein HPr.";
RL   Eur. J. Biochem. 75:275-286(1977).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=3060316;
RA   Reizer J., Saier M.H. Jr., Deutscher J., Grenier F., Thompson J.,
RA   Hengstenberg W.;
RT   "The phosphoenolpyruvate:sugar phosphotransferase system in Gram-
RT   positive bacteria: properties, mechanism, and regulation.";
RL   Crit. Rev. Microbiol. 15:297-338(1988).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=1932039; DOI=10.1021/bi00110a024;
RA   Kalbitzer H.R., Neidig K.-P., Hengstenberg W.;
RT   "Two-dimensional 1H NMR studies on HPr protein from Staphylococcus
RT   aureus: complete sequential assignments and secondary structure.";
RL   Biochemistry 30:11186-11192(1991).
RN   [5]
RP   STRUCTURE BY NMR.
RX   PubMed=8365407; DOI=10.1111/j.1432-1033.1993.tb18134.x;
RA   Kalbitzer H.R., Hengstenberg W.;
RT   "The solution structure of the histidine-containing protein (HPr) from
RT   Staphylococcus aureus as determined by two-dimensional 1H-NMR
RT   spectroscopy.";
RL   Eur. J. Biochem. 216:205-214(1993).
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).
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).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the HPr family.
CC   -!- SIMILARITY: Contains 1 HPr domain.
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DR   EMBL; X93205; CAA63688.1; -; Genomic_DNA.
DR   PIR; A03404; WPSAHP.
DR   PDB; 1KA5; NMR; -; A=1-88.
DR   PDBsum; 1KA5; -.
DR   ProteinModelPortal; P0A0E3; -.
DR   SMR; P0A0E3; 1-88.
DR   eggNOG; COG1925; -.
DR   EvolutionaryTrace; P0A0E3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
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; IPR001020; PTS_HPr_His_P_site.
DR   InterPro; IPR005698; PTS_HPr_prot.
DR   InterPro; IPR000032; PTS_HPr_prot-like.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Kinase;
KW   Phosphoprotein; Phosphotransferase system;
KW   Serine/threonine-protein kinase; Sugar transport; Transcription;
KW   Transcription regulation; Transferase; Transport.
FT   CHAIN         1     88       Phosphocarrier protein HPr.
FT                                /FTId=PRO_0000107878.
FT   DOMAIN        1     88       HPr.
FT   ACT_SITE     15     15       Pros-phosphohistidine intermediate.
FT   MOD_RES      46     46       Phosphoserine; by HPrK/P.
FT   STRAND        2      8
FT   HELIX        16     29
FT   STRAND       30     37
FT   STRAND       40     43
FT   HELIX        47     51
FT   TURN         52     54
FT   STRAND       60     69
FT   HELIX        70     84
SQ   SEQUENCE   88 AA;  9496 MW;  B2C6639D53226FF9 CRC64;
     MEQNSYVIID ETGIHARPAT MLVQTASKFD SDIQLEYNGK KVNLKSIMGV MSLGVGKDAE
     ITIYADGSDE SDAIQAISDV LSKEGLTK
//
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