PTHP_MYCPN
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 03-AUG-2022, entry version 131.
DE RecName: Full=Phosphocarrier protein HPr;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH; OrderedLocusNames=MPN_053; ORFNames=MP101;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
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., 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., Herrmann R.,
RA 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; DOI=10.1099/00221287-148-10-3277;
RA Steinhauer K., Jepp T., Hillen W., Stuelke J.;
RT "A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase
RT 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 (sugar
CC PTS). This major carbohydrate active-transport system catalyzes the
CC phosphorylation of incoming sugar substrates concomitantly with their
CC translocation across the cell membrane. The phosphoryl group from
CC phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier
CC protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA
CC domain.
CC -!- FUNCTION: P-Ser-HPr interacts with the catabolite control protein A
CC (CcpA), forming a complex that binds to DNA at the catabolite response
CC elements cre, operator sites preceding a large number of catabolite-
CC regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite
CC repression (CCR), a mechanism that allows bacteria to coordinate and
CC optimize the utilization of available carbon sources. P-Ser-HPr also
CC plays a role in inducer exclusion, in which it probably interacts with
CC several non-PTS permeases and inhibits their transport activity (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Phosphorylation on Ser-47 inhibits the phosphoryl
CC transfer from enzyme I to HPr. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR EMBL; U00089; AAB95749.1; -; Genomic_DNA.
DR PIR; S73427; S73427.
DR RefSeq; NP_109741.1; NC_000912.1.
DR RefSeq; WP_010874410.1; NC_000912.1.
DR AlphaFoldDB; P75061; -.
DR SMR; P75061; -.
DR STRING; 272634.MPN_053; -.
DR iPTMnet; P75061; -.
DR EnsemblBacteria; AAB95749; AAB95749; MPN_053.
DR GeneID; 66609308; -.
DR KEGG; mpn:MPN_053; -.
DR PATRIC; fig|272634.6.peg.53; -.
DR HOGENOM; CLU_136230_2_3_14; -.
DR OMA; SIMAMMM; -.
DR BioCyc; MPNE272634:G1GJ3-78-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR CDD; cd00367; PTS-HPr_like; 1.
DR Gene3D; 3.30.1340.10; -; 1.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
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 Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transcription; Transcription regulation; Transport.
FT CHAIN 1..88
FT /note="Phosphocarrier protein HPr"
FT /id="PRO_0000107864"
FT DOMAIN 1..88
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 15
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT MOD_RES 47
FT /note="Phosphoserine; by HPrK/P"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000269|PubMed:14730672"
SQ SEQUENCE 88 AA; 9495 MW; 5609A9F8F9E2C1FE CRC64;
MKKIQVVVKD PVGIHARPAS IIAGEANKFK SELKLVSPSG VEGNIKSIIN LMSLGIKQND
HITIKAEGTD EEEALNAIKA VLEKHQVI
