ID   PTHP_BACTI              Reviewed;          87 AA.
AC   Q9F166;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Phosphocarrier protein HPr;
GN   Name=ptsH;
OS   Bacillus thuringiensis subsp. israelensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP   ACTIVE SITE HIS-14, PHOSPHORYLATION AT HIS-14, AND MUTAGENESIS OF HIS-14.
RC   STRAIN=ATCC 35646 / USDA HD522;
RX   PubMed=11168390; DOI=10.1046/j.1432-1327.2001.01878.x;
RA   Khan S.R., Deutscher J., Vishwakarma R.A., Monedero V.,
RA   Banerjee-Bhatnagar N.;
RT   "The ptsH gene from Bacillus thuringiensis israelensis. Characterization of
RT   a new phosphorylation site on the protein HPr.";
RL   Eur. J. Biochem. 268:521-530(2001).
RN   [2]
RP   FUNCTION, PHOSPHORYLATION AT SER-45, AND MUTAGENESIS OF SER-45.
RC   STRAIN=ATCC 35646 / USDA HD522;
RX   PubMed=12218029; DOI=10.1128/jb.184.19.5410-5417.2002;
RA   Khan S.R., Banerjee-Bhatnagar N.;
RT   "Loss of catabolite repression function of HPr, the phosphocarrier protein
RT   of the bacterial phosphotransferase system, affects expression of the cry4A
RT   toxin gene in Bacillus thuringiensis subsp. israelensis.";
RL   J. Bacteriol. 184:5410-5417(2002).
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
CC       mediates glucose catabolite repression of cry4A toxin expression.
CC   -!- ACTIVITY REGULATION: Phosphorylation on Ser-45 inhibits the phosphoryl
CC       transfer from enzyme I to HPr. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: The form phosphorylated at the tele nitrogen (N(epsilon)2),
CC       instead of the expected pros nitrogen (N(delta)1), of His-14 is not
CC       able to transfer its phosphoryl group to the B.subtilis EIIA-Glc
CC       domain. This form may be inactive in PTS-catalyzed sugar transport or
CC       target an as yet unknown acceptor molecule in an alternative metabolic
CC       process. {ECO:0000269|PubMed:11168390, ECO:0000269|PubMed:12218029}.
CC   -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR   EMBL; AF117385; AAG49026.1; -; Genomic_DNA.
DR   RefSeq; WP_000411080.1; NZ_VEIF01000004.1.
DR   AlphaFoldDB; Q9F166; -.
DR   SMR; Q9F166; -.
DR   iPTMnet; Q9F166; -.
DR   GeneID; 58157922; -.
DR   GeneID; 64185363; -.
DR   GeneID; 67468349; -.
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; Direct protein sequencing; Phosphoprotein;
KW   Phosphotransferase system; Sugar transport; Transcription;
KW   Transcription regulation; Transport.
FT   CHAIN           1..87
FT                   /note="Phosphocarrier protein HPr"
FT                   /id="PRO_0000344795"
FT   DOMAIN          1..87
FT                   /note="HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT   ACT_SITE        14
FT                   /note="Pros-phosphohistidine intermediate; alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT   MOD_RES         14
FT                   /note="Tele-phosphohistidine; alternate"
FT                   /evidence="ECO:0000269|PubMed:11168390"
FT   MOD_RES         45
FT                   /note="Phosphoserine; by HPrK/P"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT                   ECO:0000269|PubMed:12218029"
FT   MUTAGEN         14
FT                   /note="H->A: Not histidine-phosphorylated."
FT                   /evidence="ECO:0000269|PubMed:11168390"
FT   MUTAGEN         45
FT                   /note="S->A: Not serine-phosphorylated. Absence of glucose-
FT                   induced cry4A expression repression. 60 to 70% reduction in
FT                   the sporulation efficiency."
FT                   /evidence="ECO:0000269|PubMed:12218029"
SQ   SEQUENCE   87 AA;  9238 MW;  340665CB95716AC0 CRC64;
     MEKIFKVTSD SGIHARPATL LVNTASKFGS DINLEYNGKN VNLKSIMGVM SLGIQQNAEI
     KITANGDDAA QALAAIEETM KNEGLGE