PTHP_PRIMG
ID PTHP_PRIMG Reviewed; 88 AA.
AC O69250;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Phosphocarrier protein HPr;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH;
OS Priestia megaterium (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WH348;
RA Wagner A., Kuester E., Hillen W.;
RT "Sequence of ptsH and ptsI of Bacillus megaterium.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND PHOSPHORYLATION AT SER-46.
RX PubMed=15369672; DOI=10.1016/j.cell.2004.08.027;
RA Schumacher M.A., Allen G.S., Diel M., Seidel G., Hillen W., Brennan R.G.;
RT "Structural basis for allosteric control of the transcription regulator
RT CcpA by the phosphoprotein HPr-Ser46-P.";
RL Cell 118:731-741(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND PHOSPHORYLATION AT SER-46.
RX PubMed=17376479; DOI=10.1016/j.jmb.2007.02.054;
RA Schumacher M.A., Seidel G., Hillen W., Brennan R.G.;
RT "Structural mechanism for the fine-tuning of CcpA function by the small
RT molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate.";
RL J. Mol. Biol. 368:1042-1050(2007).
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; AJ005075; CAA06331.1; -; Genomic_DNA.
DR RefSeq; WP_013056011.1; NZ_WIPB01000018.1.
DR PDB; 1RZR; X-ray; 2.80 A; L/S/T/Y=1-88.
DR PDB; 2NZU; X-ray; 2.50 A; L=1-88.
DR PDB; 2NZV; X-ray; 3.00 A; L=1-88.
DR PDB; 2OEN; X-ray; 3.17 A; L=1-88.
DR PDBsum; 1RZR; -.
DR PDBsum; 2NZU; -.
DR PDBsum; 2NZV; -.
DR PDBsum; 2OEN; -.
DR AlphaFoldDB; O69250; -.
DR SMR; O69250; -.
DR iPTMnet; O69250; -.
DR GeneID; 48011925; -.
DR GeneID; 64144728; -.
DR OMA; SIMAMMM; -.
DR EvolutionaryTrace; O69250; -.
DR PRO; PR:O69250; -.
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_0000107839"
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 ECO:0000269|PubMed:15369672, ECO:0000269|PubMed:17376479"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2NZU"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:2NZU"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:2NZU"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2NZU"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:2NZU"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:2NZU"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:2NZU"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1RZR"
SQ SEQUENCE 88 AA; 9119 MW; 4EDC85C2E0B9AA3B CRC64;
MAQKTFTVTA DSGIHARPAT TLVQAASKFD SDINLEFNGK TVNLKSIMGV MSLGIQKGAT
ITISAEGSDE ADALAALEDT MSKEGLGE
