ID PTHP_MYCPN Reviewed; 88 AA.
AC P75061;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 01-MAY-2013, entry version 93.
DE RecName: Full=Phosphocarrier protein HPr;
DE EC=2.7.11.-;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH; OrderedLocusNames=MPN_053; ORFNames=MP101;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
RA Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=11271496;
RX DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6;
RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M.,
RA Herrmann R., Frank R.;
RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL Electrophoresis 21:3765-3780(2000).
RN [3]
RP PHOSPHORYLATION.
RX PubMed=12368461;
RA Steinhauer K., Jepp T., Hillen W., Stuelke J.;
RT "A novel mode of control of Mycoplasma pneumoniae HPr
RT kinase/phosphatase activity reflects its parasitic lifestyle.";
RL Microbiology 148:3277-3284(2002).
RN [4]
RP PHOSPHORYLATION AT SER-47, AND MASS SPECTROMETRY.
RX PubMed=14730672; DOI=10.1002/pmic.200300511;
RA Jaffe J.D., Berg H.C., Church G.M.;
RT "Proteogenomic mapping as a complementary method to perform genome
RT annotation.";
RL Proteomics 4:59-77(2004).
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-47 inhibits the
CC phosphoryl transfer from enzyme I to HPr (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the HPr family.
CC -!- SIMILARITY: Contains 1 HPr domain.
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DR EMBL; U00089; AAB95749.1; -; Genomic_DNA.
DR PIR; S73427; S73427.
DR RefSeq; NP_109741.1; NC_000912.1.
DR ProteinModelPortal; P75061; -.
DR STRING; 272634.MPN053; -.
DR PaxDb; P75061; -.
DR EnsemblBacteria; AAB95749; AAB95749; MPN_053.
DR GeneID; 876864; -.
DR KEGG; mpn:MPN053; -.
DR PATRIC; 20021383; VBIMycPne110_0053.
DR eggNOG; COG1925; -.
DR KO; K11189; -.
DR OMA; YITAEAS; -.
DR ProtClustDB; CLSK542113; -.
DR BioCyc; MPNE272634:GJ6Z-55-MONOMER; -.
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 Complete proteome; Cytoplasm; Direct protein sequencing; Kinase;
KW Phosphoprotein; Phosphotransferase system; Reference proteome;
KW Serine/threonine-protein kinase; Sugar transport; Transcription;
KW Transcription regulation; Transferase; Transport.
FT CHAIN 1 88 Phosphocarrier protein HPr.
FT /FTId=PRO_0000107864.
FT DOMAIN 1 88 HPr.
FT ACT_SITE 15 15 Pros-phosphohistidine intermediate (By
FT similarity).
FT MOD_RES 47 47 Phosphoserine; by HPrK/P.
SQ SEQUENCE 88 AA; 9495 MW; 5609A9F8F9E2C1FE CRC64;
MKKIQVVVKD PVGIHARPAS IIAGEANKFK SELKLVSPSG VEGNIKSIIN LMSLGIKQND
HITIKAEGTD EEEALNAIKA VLEKHQVI
//
