ID   PTHP_STREI              Reviewed;          87 AA.
AC   Q9WXK8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Phosphocarrier protein HPr;
DE   AltName: Full=Histidine-containing protein;
GN   Name=ptsH;
OS   Streptococcus equinus (Streptococcus bovis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MUTAGENESIS OF
RP   SER-46.
RC   STRAIN=ATCC 700410 / JB1;
RX   PubMed=12610726; DOI=10.1007/s00203-003-0516-9;
RA   Asanuma N., Hino T.;
RT   "Molecular characterization of HPr and related enzymes, and regulation of
RT   HPr phosphorylation in the ruminal bacterium Streptococcus bovis.";
RL   Arch. Microbiol. 179:205-213(2003).
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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Transcription of ptsH appears to be regulated in response to
CC       sugars supplied, i.e. is four-fold lower when cells were grown on
CC       lactose than when grown on glucose.
CC   -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR   EMBL; AB027569; BAA78048.1; -; Genomic_DNA.
DR   RefSeq; WP_003064009.1; NZ_SPDR01000001.1.
DR   AlphaFoldDB; Q9WXK8; -.
DR   SMR; Q9WXK8; -.
DR   STRING; 1335.A6J79_06890; -.
DR   GeneID; 64018463; -.
DR   GeneID; 66897141; -.
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; Phosphoprotein; Phosphotransferase system; Sugar transport;
KW   Transcription; Transcription regulation; Transport.
FT   CHAIN           1..87
FT                   /note="Phosphocarrier protein HPr"
FT                   /id="PRO_0000107881"
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   MUTAGEN         46
FT                   /note="S->A: No phosphorylation by HPrK/P."
FT                   /evidence="ECO:0000269|PubMed:12610726"
SQ   SEQUENCE   87 AA;  8937 MW;  77D1E691843035AE CRC64;
     MASKDFHIVA ETGIHARPAT LLVQTASKFA SDITLDYKGK AVNLKSIMGV MSLGVGQGAD
     VTISAEGADA DDALAAIEET MTKEGLA