PTHP_ENTFA
ID PTHP_ENTFA Reviewed; 88 AA.
AC P07515;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Phosphocarrier protein HPr;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH; OrderedLocusNames=EF_0709;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Reizer J., Mitchell W.J., Romano A.H., Mirkov E.T., Saier M.H. Jr.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=3098288; DOI=10.1021/bi00369a031;
RA Deutscher J., Pevec B., Beyreuther K., Kiltz H.H., Hengstenberg W.;
RT "Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: amino
RT acid sequence and site of ATP-dependent phosphorylation of HPr.";
RL Biochemistry 25:6543-6551(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=8421502; DOI=10.1038/361094a0;
RA Jia Z., Vandonselaar M., Quail J.W., Delbaere L.T.J.;
RT "Active-centre torsion-angle strain revealed in 1.6 A-resolution structure
RT of histidine-containing phosphocarrier protein.";
RL Nature 361:94-97(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=11054290; DOI=10.1006/jmbi.2000.4166;
RA Audette G.F., Engelmann R., Hengstenberg W., Deutscher J., Hayakawa K.,
RA Quail J.W., Delbaere L.T.;
RT "The 1.9-A resolution structure of phospho-serine 46 HPr from Enterococcus
RT faecalis.";
RL J. Mol. Biol. 303:545-553(2000).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=9523711; DOI=10.1046/j.1432-1327.1998.2520051.x;
RA Hahmann M., Maurer T., Lorenz M., Hengstenberg W., Glaser S.,
RA Kalbitzer H.R.;
RT "Structural studies of histidine-containing phosphocarrier protein from
RT Enterococcus faecalis.";
RL Eur. J. Biochem. 252:51-58(1998).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=11168402; DOI=10.1046/j.1432-1327.2001.01916.x;
RA Maurer T., Doeker R., Goerler A., Hengstenberg W., Kalbitzer H.R.;
RT "Three-dimensional structure of the histidine-containing phosphocarrier
RT protein (HPr) from Enterococcus faecalis in solution.";
RL Eur. J. Biochem. 268:635-644(2001).
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.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR EMBL; Z19137; CAA79533.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO80530.1; -; Genomic_DNA.
DR PIR; A25053; WQSOHP.
DR RefSeq; NP_814460.1; NC_004668.1.
DR RefSeq; WP_002355551.1; NZ_KE136527.1.
DR PDB; 1FU0; X-ray; 1.90 A; A/B=1-87.
DR PDB; 1PTF; X-ray; 1.60 A; A=1-88.
DR PDB; 1QFR; NMR; -; A=1-88.
DR PDBsum; 1FU0; -.
DR PDBsum; 1PTF; -.
DR PDBsum; 1QFR; -.
DR AlphaFoldDB; P07515; -.
DR BMRB; P07515; -.
DR SMR; P07515; -.
DR STRING; 226185.EF_0709; -.
DR DrugBank; DB04522; Dexfosfoserine.
DR EnsemblBacteria; AAO80530; AAO80530; EF_0709.
DR KEGG; efa:EF0709; -.
DR PATRIC; fig|226185.45.peg.2651; -.
DR eggNOG; COG1925; Bacteria.
DR HOGENOM; CLU_136230_2_1_9; -.
DR OMA; SIMAMMM; -.
DR EvolutionaryTrace; P07515; -.
DR Proteomes; UP000001415; 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; 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_0000107853"
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 46
FT /note="Phosphoserine; by HPrK/P"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT CONFLICT 88
FT /note="E -> EQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1PTF"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1PTF"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1PTF"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1PTF"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1PTF"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1PTF"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1PTF"
SQ SEQUENCE 88 AA; 9321 MW; D01E27D6CEE6DA06 CRC64;
MEKKEFHIVA ETGIHARPAT LLVQTASKFN SDINLEYKGK SVNLKSIMGV MSLGVGQGSD
VTITVDGADE AEGMAAIVET LQKEGLAE
