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Phosphocarrier protein HPr (EC 2.7.11.-) (Histidine-containing protein)

 PTHP_MYCCT              Reviewed;          89 AA.
P45611; Q2SRD7;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 141.
RecName: Full=Phosphocarrier protein HPr;
AltName: Full=Histidine-containing protein;
Name=ptsH; OrderedLocusNames=MCAP_0716;
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC
27343 / NCTC 10154).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=340047;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8253782;
Zhu P.-P., Reizer J., Reizer A., Peterkofsky A.;
"Unique monocistronic operon (ptsH) in Mycoplasma capricolum encoding
the phosphocarrier protein, HPr, of the phosphoenolpyruvate:sugar
phosphotransferase system. Cloning, sequencing, and characterization
of ptsH.";
J. Biol. Chem. 268:26531-26540(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=California kid / ATCC 27343 / NCTC 10154;
Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C.,
Nierman W.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
3D-STRUCTURE MODELING.
PubMed=8710835; DOI=10.1002/prot.340230316;
Church W.B., Palmer A., Wathey J.C., Kitson D.H.;
"Homology modeling of histidine-containing phosphocarrier protein and
eosinophil-derived neurotoxin: construction of models and comparison
with experiment.";
Proteins 23:422-430(1995).
[4]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=7582895; DOI=10.1016/S0969-2126(01)00213-1;
Pieper U., Kapadia G., Zhu P.-P., Peterkofsky A., Herzberg O.;
"Structural evidence for the evolutionary divergence of mycoplasma
from Gram-positive bacteria: the histidine-containing phosphocarrier
protein.";
Structure 3:781-790(1995).
-!- FUNCTION: General (non sugar-specific) component of the
phosphoenolpyruvate-dependent sugar phosphotransferase system
(sugar PTS). This major carbohydrate active-transport system
catalyzes the phosphorylation of incoming sugar substrates
concomitantly with their translocation across the cell membrane.
The phosphoryl group from phosphoenolpyruvate (PEP) is transferred
to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr
then transfers it to the PTS EIIA domain.
-!- FUNCTION: P-Ser-HPr interacts with the catabolite control protein
A (CcpA), forming a complex that binds to DNA at the catabolite
response elements cre, operator sites preceding a large number of
catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in
carbon catabolite repression (CCR), a mechanism that allows
bacteria to coordinate and optimize the utilization of available
carbon sources. P-Ser-HPr also plays a role in inducer exclusion,
in which it probably interacts with several non-PTS permeases and
inhibits their transport activity (By similarity). {ECO:0000250}.
-!- ENZYME REGULATION: Phosphorylation on Ser-46 inhibits the
phosphoryl transfer from enzyme I to HPr. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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EMBL; L22432; AAA16213.1; -; Unassigned_DNA.
EMBL; CP000123; ABC01760.1; -; Genomic_DNA.
PIR; A49683; A49683.
RefSeq; WP_011387560.1; NC_007633.1.
PDB; 1PCH; X-ray; 1.80 A; A=2-89.
PDBsum; 1PCH; -.
ProteinModelPortal; P45611; -.
SMR; P45611; -.
EnsemblBacteria; ABC01760; ABC01760; MCAP_0716.
GeneID; 23778330; -.
KEGG; mcp:MCAP_0716; -.
HOGENOM; HOG000278399; -.
KO; K11189; -.
OMA; AEVWVTR; -.
OrthoDB; POG091H03ED; -.
EvolutionaryTrace; P45611; -.
Proteomes; UP000001928; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00367; PTS-HPr_like; 1.
Gene3D; 3.30.1340.10; -; 1.
InterPro; IPR000032; HPr-like.
InterPro; IPR035895; HPr-like_sf.
InterPro; IPR001020; PTS_HPr_His_P_site.
InterPro; IPR002114; PTS_HPr_Ser_P_site.
Pfam; PF00381; PTS-HPr; 1.
PRINTS; PR00107; PHOSPHOCPHPR.
SUPFAM; SSF55594; SSF55594; 1.
TIGRFAMs; TIGR01003; PTS_HPr_family; 1.
PROSITE; PS51350; PTS_HPR_DOM; 1.
PROSITE; PS00369; PTS_HPR_HIS; 1.
PROSITE; PS00589; PTS_HPR_SER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Phosphoprotein;
Phosphotransferase system; Sugar transport; Transcription;
Transcription regulation; Transport.
INIT_MET 1 1 Removed.
CHAIN 2 89 Phosphocarrier protein HPr.
/FTId=PRO_0000107862.
DOMAIN 2 89 HPr. {ECO:0000255|PROSITE-
ProRule:PRU00681}.
ACT_SITE 15 15 Pros-phosphohistidine intermediate.
MOD_RES 46 46 Phosphoserine; by HPrK/P.
{ECO:0000255|PROSITE-ProRule:PRU00681}.
STRAND 3 7 {ECO:0000244|PDB:1PCH}.
HELIX 16 26 {ECO:0000244|PDB:1PCH}.
STRAND 30 37 {ECO:0000244|PDB:1PCH}.
STRAND 40 43 {ECO:0000244|PDB:1PCH}.
HELIX 47 53 {ECO:0000244|PDB:1PCH}.
STRAND 60 67 {ECO:0000244|PDB:1PCH}.
HELIX 70 83 {ECO:0000244|PDB:1PCH}.
SEQUENCE 89 AA; 9418 MW; 9E5CFF9278028F49 CRC64;
MAKFSAIITD KVGLHARPAS VLAKEASKFS SNITIIANEK QGNLKSIMNV MAMAIKTGTE
ITIQADGNDA DQAIQAIKQT MIDTALIQG


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