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Database: UniProt
Entry: P75061
LinkDB: P75061
Original site: P75061 
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-OCT-2014, entry version 101.
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 IDENTIFICATION BY 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). {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-47 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; 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; REDEKIN; -.
DR   OrthoDB; EOG6XDGX2; -.
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: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   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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00681}.
FT   ACT_SITE     15     15       Pros-phosphohistidine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00681}.
FT   MOD_RES      47     47       Phosphoserine; by HPrK/P.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00681,
FT                                ECO:0000269|PubMed:12368461,
FT                                ECO:0000269|PubMed:14730672}.
SQ   SEQUENCE   88 AA;  9495 MW;  5609A9F8F9E2C1FE CRC64;
     MKKIQVVVKD PVGIHARPAS IIAGEANKFK SELKLVSPSG VEGNIKSIIN LMSLGIKQND
     HITIKAEGTD EEEALNAIKA VLEKHQVI
//
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