PTHP_MYCCT
ID PTHP_MYCCT Reviewed; 89 AA.
AC P45611; Q2SRD7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=Phosphocarrier protein HPr;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH; OrderedLocusNames=MCAP_0716;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8253782; DOI=10.1016/s0021-9258(19)74345-2;
RA Zhu P.-P., Reizer J., Reizer A., Peterkofsky A.;
RT "Unique monocistronic operon (ptsH) in Mycoplasma capricolum encoding the
RT phosphocarrier protein, HPr, of the phosphoenolpyruvate:sugar
RT phosphotransferase system. Cloning, sequencing, and characterization of
RT ptsH.";
RL J. Biol. Chem. 268:26531-26540(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP 3D-STRUCTURE MODELING.
RX PubMed=8710835; DOI=10.1002/prot.340230316;
RA Church W.B., Palmer A., Wathey J.C., Kitson D.H.;
RT "Homology modeling of histidine-containing phosphocarrier protein and
RT eosinophil-derived neurotoxin: construction of models and comparison with
RT experiment.";
RL Proteins 23:422-430(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=7582895; DOI=10.1016/s0969-2126(01)00213-1;
RA Pieper U., Kapadia G., Zhu P.-P., Peterkofsky A., Herzberg O.;
RT "Structural evidence for the evolutionary divergence of mycoplasma from
RT Gram-positive bacteria: the histidine-containing phosphocarrier protein.";
RL Structure 3:781-790(1995).
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-46 inhibits the phosphoryl
CC transfer from enzyme I to HPr. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR EMBL; L22432; AAA16213.1; -; Unassigned_DNA.
DR EMBL; CP000123; ABC01760.1; -; Genomic_DNA.
DR PIR; A49683; A49683.
DR RefSeq; WP_011387560.1; NC_007633.1.
DR PDB; 1PCH; X-ray; 1.80 A; A=2-89.
DR PDBsum; 1PCH; -.
DR AlphaFoldDB; P45611; -.
DR SMR; P45611; -.
DR EnsemblBacteria; ABC01760; ABC01760; MCAP_0716.
DR GeneID; 23778330; -.
DR KEGG; mcp:MCAP_0716; -.
DR HOGENOM; CLU_136230_2_0_14; -.
DR OMA; SIMAMMM; -.
DR OrthoDB; 404807at2; -.
DR PhylomeDB; P45611; -.
DR EvolutionaryTrace; P45611; -.
DR Proteomes; UP000001928; 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 3D-structure; Cytoplasm; Phosphoprotein; Phosphotransferase system;
KW Sugar transport; Transcription; Transcription regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..89
FT /note="Phosphocarrier protein HPr"
FT /id="PRO_0000107862"
FT DOMAIN 2..89
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 15
FT /note="Pros-phosphohistidine intermediate"
FT MOD_RES 46
FT /note="Phosphoserine; by HPrK/P"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1PCH"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1PCH"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1PCH"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1PCH"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1PCH"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1PCH"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1PCH"
SQ SEQUENCE 89 AA; 9418 MW; 9E5CFF9278028F49 CRC64;
MAKFSAIITD KVGLHARPAS VLAKEASKFS SNITIIANEK QGNLKSIMNV MAMAIKTGTE
ITIQADGNDA DQAIQAIKQT MIDTALIQG
