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 03-APR-2013, entry version 51.
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-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; 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; HPr_protein; 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
//
