ID   PTHP_STRMU              Reviewed;          87 AA.
AC   P45596;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Phosphocarrier protein HPr;
DE   AltName: Full=Histidine-containing protein;
GN   Name=ptsH; OrderedLocusNames=SMU_674;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NG5 / Serotype c;
RX   PubMed=8132321; DOI=10.1128/iai.62.4.1156-1165.1994;
RA   Boyd D.A., Cvitkovitch D.G., Hamilton I.R.;
RT   "Sequence and expression of the genes for HPr (ptsH) and enzyme I (ptsI) of
RT   the phosphoenolpyruvate-dependent phosphotransferase transport system from
RT   Streptococcus mutans.";
RL   Infect. Immun. 62:1156-1165(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-87.
RC   STRAIN=Ingbritt;
RX   PubMed=8147873; DOI=10.1006/bbrc.1994.1372;
RA   Dashper S.G., Kirszbaum L., Huq N.L., Riley P.F., Reynolds E.C.;
RT   "Complete amino acid sequence and comparative molecular modelling of HPr
RT   from Streptococcus mutans Ingbritt.";
RL   Biochem. Biophys. Res. Commun. 199:1297-1304(1994).
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; L15191; AAA91092.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN58408.1; -; Genomic_DNA.
DR   PIR; A44562; A44562.
DR   RefSeq; NP_721102.1; NC_004350.2.
DR   RefSeq; WP_002262984.1; NC_004350.2.
DR   AlphaFoldDB; P45596; -.
DR   SMR; P45596; -.
DR   STRING; 210007.SMU_674; -.
DR   PRIDE; P45596; -.
DR   EnsemblBacteria; AAN58408; AAN58408; SMU_674.
DR   GeneID; 66817866; -.
DR   KEGG; smu:SMU_674; -.
DR   PATRIC; fig|210007.7.peg.599; -.
DR   eggNOG; COG1925; Bacteria.
DR   HOGENOM; CLU_136230_2_1_9; -.
DR   OMA; SIMAMMM; -.
DR   PhylomeDB; P45596; -.
DR   Proteomes; UP000002512; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8147873"
FT   CHAIN           2..87
FT                   /note="Phosphocarrier protein HPr"
FT                   /id="PRO_0000107883"
FT   DOMAIN          2..87
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"
SQ   SEQUENCE   87 AA;  8936 MW;  77AF0191843464AB CRC64;
     MASKDFHIVA ETGIHARPAT LLVQTASKFA SDITLDYKGK AVNLKSIMGV MSLGVGQGAD
     VTITAEGADA DDAIAAINET MTKEGLA