ID   PTHP_STRSL              Reviewed;          87 AA.
AC   P24366;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Phosphocarrier protein HPr;
DE   AltName: Full=Histidine-containing protein;
GN   Name=ptsH;
OS   Streptococcus salivarius.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25975;
RX   PubMed=8294015; DOI=10.1016/0378-1119(93)90443-7;
RA   Gagnon G., Vadeboncoeur C., Frenette M.;
RT   "Phosphotransferase system of Streptococcus salivarius: characterization of
RT   the ptsH gene and its product.";
RL   Gene 136:27-34(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-20.
RX   PubMed=1799636; DOI=10.1016/0300-9084(91)90174-y;
RA   Vadeboncoeur C., Konishi Y., Dumas F., Gauthier L., Frenette M.;
RT   "HPr polymorphism in oral streptococci is caused by the partial removal of
RT   the N-terminal methionine.";
RL   Biochimie 73:1427-1430(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-87.
RX   PubMed=1427100; DOI=10.1016/0378-1119(92)90163-j;
RA   Gagnon G., Vadeboncoeur C., Levesque R.C., Frenette M.;
RT   "Cloning, sequencing and expression in Escherichia coli of the ptsI gene
RT   encoding enzyme I of the phosphoenolpyruvate:sugar phosphotransferase
RT   transport system from Streptococcus salivarius.";
RL   Gene 121:71-78(1992).
RN   [4]
RP   PHOSPHORYLATION AT SER-46.
RC   STRAIN=ATCC 25975;
RX   PubMed=9922231; DOI=10.1128/jb.181.3.709-717.1999;
RA   Brochu D., Vadeboncoeur C.;
RT   "The HPr(Ser) kinase of Streptococcus salivarius: purification, properties,
RT   and cloning of the hprK gene.";
RL   J. Bacteriol. 181:709-717(1999).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR   EMBL; Z17217; CAA78923.1; -; Genomic_DNA.
DR   EMBL; M81756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A48400; A48400.
DR   PIR; B48400; B48400.
DR   PIR; S37585; S37585.
DR   RefSeq; WP_045772118.1; NZ_WMYH01000035.1.
DR   AlphaFoldDB; P24366; -.
DR   SMR; P24366; -.
DR   STRING; 1304.HMPREF3219_0201232; -.
DR   iPTMnet; P24366; -.
DR   SABIO-RK; P24366; -.
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; Sugar transport; Transcription;
KW   Transcription regulation; Transport.
FT   CHAIN           1..87
FT                   /note="Phosphocarrier protein HPr"
FT                   /id="PRO_0000107885"
FT   DOMAIN          1..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,
FT                   ECO:0000269|PubMed:9922231"
FT   VARIANT         1
FT                   /note="Missing (in some of the molecules)"
SQ   SEQUENCE   87 AA;  8907 MW;  77D4F29196BF64AE CRC64;
     MASKDFHIVA ETGIHARPAT LLVQTASKFA SDITLDYKGK AVNLKSIMGV MSLGVGQGAD
     VTISAEGADA DDAIVAIAET MTKEGLA