ID   PTHP_LACLA              Reviewed;          88 AA.
AC   Q9CJ83;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Phosphocarrier protein HPr;
DE   AltName: Full=Histidine-containing protein;
GN   Name=ptsH; OrderedLocusNames=LL0117; ORFNames=L120335;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
RN   [2]
RP   PHOSPHORYLATION AT SER-46, AND MUTAGENESIS OF SER-46.
RX   PubMed=11344147; DOI=10.1128/jb.183.11.3391-3398.2001;
RA   Monedero V., Kuipers O.P., Jamet E., Deutscher J.;
RT   "Regulatory functions of serine-46-phosphorylated HPr in Lactococcus
RT   lactis.";
RL   J. Bacteriol. 183:3391-3398(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. {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; AE005176; AAK04215.1; -; Genomic_DNA.
DR   PIR; E86639; E86639.
DR   RefSeq; NP_266273.1; NC_002662.1.
DR   RefSeq; WP_010905128.1; NC_002662.1.
DR   AlphaFoldDB; Q9CJ83; -.
DR   SMR; Q9CJ83; -.
DR   STRING; 272623.L120335; -.
DR   iPTMnet; Q9CJ83; -.
DR   PaxDb; Q9CJ83; -.
DR   EnsemblBacteria; AAK04215; AAK04215; L120335.
DR   KEGG; lla:L120335; -.
DR   PATRIC; fig|272623.7.peg.131; -.
DR   eggNOG; COG1925; Bacteria.
DR   HOGENOM; CLU_136230_2_1_9; -.
DR   OMA; SIMAMMM; -.
DR   Proteomes; UP000002196; 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; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transcription; Transcription regulation; Transport.
FT   CHAIN           1..88
FT                   /note="Phosphocarrier protein HPr"
FT                   /id="PRO_0000107857"
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                   ECO:0000269|PubMed:11344147"
FT   MUTAGEN         46
FT                   /note="S->A: Abolished S-46 phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:11344147"
SQ   SEQUENCE   88 AA;  9179 MW;  1C5841F72CDB435C CRC64;
     MASKEFHIVV ETGIHARPAT LLVHTASKFT SEITLEYKGK SVNLKSIMGV MSLGVGQGAD
     VTISAEGADA DDAISTIAET MTKEGLAE