ID   PTHP_LACCA              Reviewed;          88 AA.
AC   Q9KJV3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Phosphocarrier protein HPr;
DE   AltName: Full=Histidine-containing protein;
GN   Name=ptsH;
OS   Lactobacillus casei.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 393 / DSM 20011 / BCRC 10697 / JCM 1134 / NBRC 15883 / NCIMB
RC   11970 / NCDO 161 / WDCM 00100;
RX   PubMed=10844647; DOI=10.1046/j.1365-2958.2000.01862.x;
RA   Viana R., Monedero V., Dossonnet V., Vadeboncoeur C., Perez-Martinez G.,
RA   Deutscher J.;
RT   "Enzyme I and HPr from Lactobacillus casei: their role in sugar transport,
RT   carbon catabolite repression and inducer exclusion.";
RL   Mol. Microbiol. 36:570-584(2000).
RN   [2]
RP   PHOSPHORYLATION AT SER-46.
RC   STRAIN=ATCC 393 / DSM 20011 / BCRC 10697 / JCM 1134 / NBRC 15883 / NCIMB
RC   11970 / NCDO 161 / WDCM 00100;
RX   PubMed=10762262; DOI=10.1128/jb.182.9.2582-2590.2000;
RA   Dossonnet V., Monedero V., Zagorec M., Galinier A., Perez-Martinez G.,
RA   Deutscher J.;
RT   "Phosphorylation of HPr by the bifunctional HPr kinase/P-Ser-HPr
RT   phosphatase from Lactobacillus casei controls catabolite repression and
RT   inducer exclusion but not inducer expulsion.";
RL   J. Bacteriol. 182:2582-2590(2000).
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. {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR   EMBL; AF159589; AAF74346.1; -; Genomic_DNA.
DR   RefSeq; WP_003566007.1; NZ_WBOC01000006.1.
DR   AlphaFoldDB; Q9KJV3; -.
DR   SMR; Q9KJV3; -.
DR   STRING; 1582.AAW28_12415; -.
DR   iPTMnet; Q9KJV3; -.
DR   GeneID; 61269955; -.
DR   eggNOG; COG1925; Bacteria.
DR   OMA; SIMAMMM; -.
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..88
FT                   /note="Phosphocarrier protein HPr"
FT                   /id="PRO_0000107856"
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:0000305|PubMed:10762262"
SQ   SEQUENCE   88 AA;  9254 MW;  5723EBB1345F56CA CRC64;
     MEKREFNIIA ETGIHARPAT LLVQAASKFN SDINLEYKGK SVNLKSIMGV MSLGVGQGAD
     VTISAEGADE ADAIAAITDT MKKEGLAE