ID   PTHP_STAXY              Reviewed;          88 AA.
AC   Q9EYQ9;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Phosphocarrier protein HPr;
DE   AltName: Full=Histidine-containing protein;
GN   Name=ptsH;
OS   Staphylococcus xylosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 20267 / Isolate C2A;
RA   Jankovic I., Meyer J., Brueckner R.;
RT   "Contribution of the phosphotransferase system to catabolite control
RT   protein A-dependent repression in Staphylococcus xylosus.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION AT SER-46.
RC   STRAIN=DSM 20267 / Isolate C2A;
RX   PubMed=10714994; DOI=10.1128/jb.182.7.1895-1902.2000;
RA   Huynh P.L., Jankovic I., Schnell N., Brueckner R.;
RT   "Characterization of an HPr kinase mutant of Staphylococcus xylosus.";
RL   J. Bacteriol. 182:1895-1902(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   -!- 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; AF316496; AAG38583.1; -; Genomic_DNA.
DR   RefSeq; WP_017724134.1; NZ_VEDS01000001.1.
DR   AlphaFoldDB; Q9EYQ9; -.
DR   SMR; Q9EYQ9; -.
DR   STRING; 1288.SXYLSMQ121_1710; -.
DR   iPTMnet; Q9EYQ9; -.
DR   GeneID; 45497370; -.
DR   eggNOG; COG1925; Bacteria.
DR   OrthoDB; 404807at2; -.
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   Transport.
FT   CHAIN           1..88
FT                   /note="Phosphocarrier protein HPr"
FT                   /id="PRO_0000107880"
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:10714994"
SQ   SEQUENCE   88 AA;  9553 MW;  5F65301655832D4F CRC64;
     MEQKSYVIID ETGIHARPAT MLVQTASKFD SDIQLEYNGK KVNLKSIMGV MSLGVGKDAE
     ITIYADGSDE TDAIEAITDI LSKEGLTK