ID   PTHP_GEOSE              Reviewed;          88 AA.
AC   P42013;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Phosphocarrier protein HPr;
DE   AltName: Full=Histidine-containing protein;
GN   Name=ptsH;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=XL-65-6;
RX   PubMed=7670643; DOI=10.1099/13500872-141-6-1443;
RA   Lai X., Ingram L.O.;
RT   "Discovery of a ptsHI operon, which includes a third gene (ptsT), in the
RT   thermophile Bacillus stearothermophilus.";
RL   Microbiology 141:1443-1449(1995).
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; U12340; AAA86048.1; -; Genomic_DNA.
DR   RefSeq; WP_011230496.1; NZ_CP034952.1.
DR   PDB; 1Y4Y; X-ray; 2.00 A; A/B/C=1-88.
DR   PDB; 1Y50; X-ray; 2.00 A; A=1-88.
DR   PDB; 1Y51; X-ray; 1.65 A; A/B/C=1-88.
DR   PDBsum; 1Y4Y; -.
DR   PDBsum; 1Y50; -.
DR   PDBsum; 1Y51; -.
DR   AlphaFoldDB; P42013; -.
DR   SMR; P42013; -.
DR   EvolutionaryTrace; P42013; -.
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   3D-structure; Cytoplasm; Phosphoprotein; Phosphotransferase system;
KW   Sugar transport; Transcription; Transcription regulation; Transport.
FT   CHAIN           1..88
FT                   /note="Phosphocarrier protein HPr"
FT                   /id="PRO_0000107841"
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         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         46
FT                   /note="Phosphoserine; by HPrK/P"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:1Y51"
FT   HELIX           16..27
FT                   /evidence="ECO:0007829|PDB:1Y51"
FT   STRAND          29..37
FT                   /evidence="ECO:0007829|PDB:1Y51"
FT   STRAND          40..43
FT                   /evidence="ECO:0007829|PDB:1Y51"
FT   HELIX           47..52
FT                   /evidence="ECO:0007829|PDB:1Y51"
FT   STRAND          60..67
FT                   /evidence="ECO:0007829|PDB:1Y51"
FT   HELIX           70..83
FT                   /evidence="ECO:0007829|PDB:1Y51"
SQ   SEQUENCE   88 AA;  9167 MW;  BD5DAE263AAF9434 CRC64;
     MAEKTFKVVS DSGIHARPAT ILVQTASKFN SEIQLEYNGK TVNLKSIMGV MSLGIPKGAT
     IKITAEGADA AEAMAALTDT LAKEGLAE