PTHP_BACSU
ID PTHP_BACSU Reviewed; 88 AA.
AC P08877;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Phosphocarrier protein HPr;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH; OrderedLocusNames=BSU13900;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=2497294; DOI=10.1111/j.1365-2958.1989.tb00109.x;
RA Gonzy-Treboul G., Zagorec M., Rain-Guion M.-C., Steinmetz M.;
RT "Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis:
RT nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and evidence for a
RT ptsHI operon.";
RL Mol. Microbiol. 3:103-112(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=1495386; DOI=10.1111/j.1365-2958.1992.tb00882.x;
RA Mitchell C., Morris P.W., Vary J.C.;
RT "Amino acid sequences of several Bacillus subtilis proteins modified by
RT apparent guanylylation.";
RL Mol. Microbiol. 6:1579-1581(1992).
RN [4]
RP PROTEIN SEQUENCE OF 2-27.
RC STRAIN=168 / JH642;
RX PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT "Cold shock stress-induced proteins in Bacillus subtilis.";
RL J. Bacteriol. 178:4611-4619(1996).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF SER-46.
RX PubMed=8195089; DOI=10.1128/jb.176.11.3336-3344.1994;
RA Deutscher J., Reizer J., Fischer C., Galinier A., Saier M.H. Jr.,
RA Steinmetz M.;
RT "Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier
RT protein of the phosphotransferase system, by mutation of the ptsH gene
RT confers catabolite repression resistance to several catabolic genes of
RT Bacillus subtilis.";
RL J. Bacteriol. 176:3336-3344(1994).
RN [6]
RP FUNCTION.
RX PubMed=8596444; DOI=10.1111/j.1365-2958.1995.mmi_17050953.x;
RA Fujita Y., Miwa Y., Galinier A., Deutscher J.;
RT "Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-
RT responsive element by a protein complex formed between CcpA and seryl-
RT phosphorylated HPr.";
RL Mol. Microbiol. 17:953-960(1995).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-46, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), ACTIVE SITE HIS-15, AND
RP PHOSPHORYLATION AT HIS-15.
RX PubMed=1549615; DOI=10.1073/pnas.89.6.2499;
RA Herzberg O., Reddy P., Sutrina S., Saier M.H. Jr., Reizer J., Kapadia G.;
RT "Structure of the histidine-containing phosphocarrier protein HPr from
RT Bacillus subtilis at 2.0-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2499-2503(1992).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS.
RX PubMed=7704530; DOI=10.1016/s0969-2126(94)00122-7;
RA Liao D.-I., Herzberg O.;
RT "Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp
RT histidine-containing phosphocarrier proteins.";
RL Structure 2:1203-1216(1994).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=2119803; DOI=10.1021/bi00483a006;
RA Wittekind M., Reizer J., Klevit R.E.;
RT "Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr:
RT use of spectra obtained from mutants to resolve spectral overlap.";
RL Biochemistry 29:7191-7200(1990).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=1303754; DOI=10.1002/pro.5560011016;
RA Wittekind M., Rajagopal P., Branchini B.R., Reizer J., Saier M.H. Jr.,
RA Klevit R.E.;
RT "Solution structure of the phosphocarrier protein HPr from Bacillus
RT subtilis by two-dimensional NMR spectroscopy.";
RL Protein Sci. 1:1363-1376(1992).
RN [12]
RP STRUCTURE BY NMR.
RX PubMed=9336834; DOI=10.1002/pro.5560061006;
RA Jones B.E., Rajagopal P., Klevit R.E.;
RT "Phosphorylation on histidine is accompanied by localized structural
RT changes in the phosphocarrier protein, HPr from Bacillus subtilis.";
RL Protein Sci. 6:2107-2119(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-88 IN COMPLEX WITH L.CASEI
RP HPRK/P.
RX PubMed=12359875; DOI=10.1073/pnas.192368699;
RA Fieulaine S., Morera S., Poncet S., Mijakovic I., Galinier A., Janin J.,
RA Deutscher J., Nessler S.;
RT "X-ray structure of a bifunctional protein kinase in complex with its
RT protein substrate HPr.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13437-13441(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 also
CC plays a role in inducer exclusion, in which it probably interacts with
CC several non-PTS permeases and inhibits their transport activity.
CC -!- ACTIVITY REGULATION: Phosphorylation on Ser-46 inhibits the phosphoryl
CC transfer from enzyme I to HPr.
CC -!- INTERACTION:
CC P08877; P25144: ccpA; NbExp=3; IntAct=EBI-1034482, EBI-5247535;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR EMBL; X12832; CAA31317.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13263.1; -; Genomic_DNA.
DR PIR; S04177; WQBSPH.
DR RefSeq; NP_389273.1; NC_000964.3.
DR RefSeq; WP_003154654.1; NZ_JNCM01000035.1.
DR PDB; 1JEM; NMR; -; A=2-88.
DR PDB; 1KKL; X-ray; 2.80 A; H/I/J=1-88.
DR PDB; 1KKM; X-ray; 2.80 A; H/I/J=1-88.
DR PDB; 1SPH; X-ray; 2.00 A; A/B=1-88.
DR PDB; 2FEP; X-ray; 2.45 A; S=2-88.
DR PDB; 2HID; NMR; -; A=2-88.
DR PDB; 2HPR; X-ray; 2.00 A; A=2-88.
DR PDB; 3OQM; X-ray; 2.96 A; D/S=2-88.
DR PDB; 3OQN; X-ray; 3.30 A; D/S=2-88.
DR PDB; 3OQO; X-ray; 2.97 A; D/S=2-88.
DR PDBsum; 1JEM; -.
DR PDBsum; 1KKL; -.
DR PDBsum; 1KKM; -.
DR PDBsum; 1SPH; -.
DR PDBsum; 2FEP; -.
DR PDBsum; 2HID; -.
DR PDBsum; 2HPR; -.
DR PDBsum; 3OQM; -.
DR PDBsum; 3OQN; -.
DR PDBsum; 3OQO; -.
DR AlphaFoldDB; P08877; -.
DR BMRB; P08877; -.
DR SMR; P08877; -.
DR IntAct; P08877; 5.
DR MINT; P08877; -.
DR STRING; 224308.BSU13900; -.
DR DrugBank; DB01899; Nd1-Phosphonohistidine.
DR iPTMnet; P08877; -.
DR jPOST; P08877; -.
DR PaxDb; P08877; -.
DR PRIDE; P08877; -.
DR EnsemblBacteria; CAB13263; CAB13263; BSU_13900.
DR GeneID; 66326619; -.
DR GeneID; 939259; -.
DR KEGG; bsu:BSU13900; -.
DR PATRIC; fig|224308.179.peg.1516; -.
DR eggNOG; COG1925; Bacteria.
DR InParanoid; P08877; -.
DR OMA; SIMAMMM; -.
DR PhylomeDB; P08877; -.
DR BioCyc; BSUB:BSU13900-MON; -.
DR EvolutionaryTrace; P08877; -.
DR PRO; PR:P08877; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0043610; P:regulation of carbohydrate utilization; IMP:CACAO.
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; Direct protein sequencing; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transcription; Transcription regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1495386,
FT ECO:0000269|PubMed:8755892"
FT CHAIN 2..88
FT /note="Phosphocarrier protein HPr"
FT /id="PRO_0000107842"
FT DOMAIN 2..88
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 15
FT /note="Pros-phosphohistidine intermediate; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000269|PubMed:1549615"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MOD_RES 15
FT /note="Tele-phosphohistidine; alternate"
FT /evidence="ECO:0000269|PubMed:1549615"
FT MOD_RES 46
FT /note="Phosphoserine; by HPrK/P"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000269|PubMed:17218307"
FT MUTAGEN 46
FT /note="S->A: No phosphorylation by HPrK/P; abolishes the
FT catabolite repressive effects of glucose on gluconate
FT kinase, glucitol dehydrogenase, and the mannitol-specific
FT catabolic enzymes."
FT /evidence="ECO:0000269|PubMed:8195089"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1SPH"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3OQN"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1SPH"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:1SPH"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1SPH"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1SPH"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1SPH"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1SPH"
SQ SEQUENCE 88 AA; 9189 MW; 2B13DBD63DD636A9 CRC64;
MAQKTFKVTA DSGIHARPAT VLVQTASKYD ADVNLEYNGK TVNLKSIMGV MSLGIAKGAE
ITISASGADE NDALNALEET MKSEGLGE
