PTHP_STACA
ID PTHP_STACA Reviewed; 88 AA.
AC P23534;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Phosphocarrier protein HPr;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH;
OS Staphylococcus carnosus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1281;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1901791; DOI=10.1111/j.1432-1033.1991.tb15875.x;
RA Eisermann R., Fischer R., Kessler U., Neubauer A., Hengstenberg W.;
RT "Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system.
RT Purification and protein sequencing of the Staphylococcus carnosus
RT histidine-containing protein, and cloning and DNA sequencing of the ptsH
RT gene.";
RL Eur. J. Biochem. 197:9-14(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-88.
RX PubMed=1551842; DOI=10.1128/jb.174.7.2208-2214.1992;
RA Kohlbrecher D., Eisermann R., Hengstenberg W.;
RT "Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system:
RT molecular cloning and nucleotide sequence of the Staphylococcus carnosus
RT ptsI gene and expression and complementation studies of the gene product.";
RL J. Bacteriol. 174:2208-2214(1992).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=10794411; DOI=10.1110/ps.9.4.693;
RA Kalbitzer H.R., Goerler A., Li H., Dubovskii P.V., Hengstenberg W.,
RA Kowolik C., Yamada H., Akasaka K.;
RT "15N and 1H NMR study of histidine containing protein (HPr) from
RT Staphylococcus carnosus at high pressure.";
RL Protein Sci. 9:693-703(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.
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; M69050; AAA26663.1; -; Genomic_DNA.
DR EMBL; X60766; CAA43175.1; -; Genomic_DNA.
DR PIR; S15367; A42374.
DR RefSeq; WP_015899958.1; NZ_LISV01000017.1.
DR PDB; 1QR5; NMR; -; A=1-88.
DR PDB; 1TXE; NMR; -; A=1-88.
DR PDBsum; 1QR5; -.
DR PDBsum; 1TXE; -.
DR AlphaFoldDB; P23534; -.
DR BMRB; P23534; -.
DR SMR; P23534; -.
DR GeneID; 60545596; -.
DR PATRIC; fig|1281.6.peg.2535; -.
DR OMA; SIMAMMM; -.
DR EvolutionaryTrace; P23534; -.
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_0000107879"
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:0000255|PROSITE-ProRule:PRU00681"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1QR5"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:1QR5"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1QR5"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1QR5"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1QR5"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:1QR5"
FT STRAND 57..69
FT /evidence="ECO:0007829|PDB:1QR5"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:1QR5"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1QR5"
SQ SEQUENCE 88 AA; 9511 MW; F5E53EF0A6ED85DF CRC64;
MEQQSYTIID ETGIHARPAT MLVQTASKFD SDIQLEYNGK KVNLKSIMGV MSLGVGKDAE
ITIYADGSDE ADAIQAITDV LSKEGLTE
