PTHP_STAAU
ID PTHP_STAAU Reviewed; 88 AA.
AC P0A0E3; P02907;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Phosphocarrier protein HPr;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=305A;
RA Kravanja M., Engelmann R., Christiansen I., Hengstenberg W.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE.
RX PubMed=862621; DOI=10.1111/j.1432-1033.1977.tb11527.x;
RA Beyreuther K., Raufuss H., Schrecker O., Hengstenberg W.;
RT "The phosphoenolpyruvate-dependent phosphotransferase system of
RT Staphylococcus aureus. 1. Amino-acid sequence of the phosphocarrier protein
RT HPr.";
RL Eur. J. Biochem. 75:275-286(1977).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=3060316; DOI=10.3109/10408418809104461;
RA Reizer J., Saier M.H. Jr., Deutscher J., Grenier F., Thompson J.,
RA Hengstenberg W.;
RT "The phosphoenolpyruvate:sugar phosphotransferase system in Gram-positive
RT bacteria: properties, mechanism, and regulation.";
RL Crit. Rev. Microbiol. 15:297-338(1988).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=1932039; DOI=10.1021/bi00110a024;
RA Kalbitzer H.R., Neidig K.-P., Hengstenberg W.;
RT "Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus:
RT complete sequential assignments and secondary structure.";
RL Biochemistry 30:11186-11192(1991).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=8365407; DOI=10.1111/j.1432-1033.1993.tb18134.x;
RA Kalbitzer H.R., Hengstenberg W.;
RT "The solution structure of the histidine-containing protein (HPr) from
RT Staphylococcus aureus as determined by two-dimensional 1H-NMR
RT spectroscopy.";
RL Eur. J. Biochem. 216:205-214(1993).
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; X93205; CAA63688.1; -; Genomic_DNA.
DR PIR; A03404; WPSAHP.
DR RefSeq; WP_000437472.1; NZ_WYDB01000003.1.
DR PDB; 1KA5; NMR; -; A=1-88.
DR PDBsum; 1KA5; -.
DR AlphaFoldDB; P0A0E3; -.
DR BMRB; P0A0E3; -.
DR SMR; P0A0E3; -.
DR GeneID; 66839278; -.
DR OMA; SIMAMMM; -.
DR EvolutionaryTrace; P0A0E3; -.
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; Direct protein sequencing; Phosphoprotein;
KW Phosphotransferase system; Sugar transport; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..88
FT /note="Phosphocarrier protein HPr"
FT /id="PRO_0000107878"
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..8
FT /evidence="ECO:0007829|PDB:1KA5"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:1KA5"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1KA5"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1KA5"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:1KA5"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1KA5"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:1KA5"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:1KA5"
SQ SEQUENCE 88 AA; 9496 MW; B2C6639D53226FF9 CRC64;
MEQNSYVIID ETGIHARPAT MLVQTASKFD SDIQLEYNGK KVNLKSIMGV MSLGVGKDAE
ITIYADGSDE SDAIQAISDV LSKEGLTK
