PTHP_ECOLI
ID PTHP_ECOLI Reviewed; 85 AA.
AC P0AA04; P05525; P07006;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Phosphocarrier protein HPr;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH; Synonyms=hpr; OrderedLocusNames=b2415, JW2408;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2457575; DOI=10.1128/jb.170.9.3827-3837.1988;
RA de Reuse H., Danchin A.;
RT "The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-
RT dependent phosphotransferase system: a complex operon with several modes of
RT transcription.";
RL J. Bacteriol. 170:3827-3837(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2411636; DOI=10.1016/0378-1119(85)90172-6;
RA de Reuse H., Roy A., Danchin A.;
RT "Analysis of the ptsH-ptsI-crr region in Escherichia coli K-12: nucleotide
RT sequence of the ptsH gene.";
RL Gene 35:199-207(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2960675; DOI=10.1016/s0021-9258(18)47721-6;
RA Saffen D.W., Presper K.A., Doering T.L., Roseman S.;
RT "Sugar transport by the bacterial phosphotransferase system. Molecular
RT cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr
RT genes.";
RL J. Biol. Chem. 262:16241-16253(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3290198; DOI=10.1128/jb.170.7.3150-3157.1988;
RA Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.;
RT "DNA sequences of the cysK regions of Salmonella typhimurium and
RT Escherichia coli and linkage of the cysK regions to ptsH.";
RL J. Bacteriol. 170:3150-3157(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [9]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [10]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [11]
RP ACTIVE SITE HIS-15.
RX PubMed=2261470; DOI=10.1021/bi00487a026;
RA van Dijk A.A., de Lange L.C., Bachovchin W.W., Robillard G.T.;
RT "Effect of phosphorylation on hydrogen-bonding interactions of the active
RT site histidine of the phosphocarrier protein HPr of the
RT phosphoenolpyruvate-dependent phosphotransferase system determined by 15N
RT NMR spectroscopy.";
RL Biochemistry 29:8164-8171(1990).
RN [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8226757; DOI=10.2210/pdb1poh/pdb;
RA Jia Z., Quail J.W., Waygood E.B., Delbaere L.T.J.;
RT "The 2.0-A resolution structure of Escherichia coli histidine-containing
RT phosphocarrier protein HPr. A redetermination.";
RL J. Biol. Chem. 268:22490-22501(1993).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=8784179; DOI=10.1021/bi9603480;
RA Napper S., Anderson J.W., Georges F., Quail J.W., Delbaere L.T.J.,
RA Waygood E.B.;
RT "Mutation of serine-46 to aspartate in the histidine-containing protein of
RT Escherichia coli mimics the inactivation by phosphorylation of serine-46 in
RT HPrs from Gram-positive bacteria.";
RL Biochemistry 35:11260-11267(1996).
RN [15]
RP STRUCTURE BY NMR.
RX PubMed=3542036; DOI=10.1021/bi00371a073;
RA Klevit R.E., Waygood E.B.;
RT "Two-dimensional 1H NMR studies of histidine-containing protein from
RT Escherichia coli. 3. Secondary and tertiary structure as determined by
RT NMR.";
RL Biochemistry 25:7774-7781(1986).
RN [16]
RP STRUCTURE BY NMR.
RX PubMed=1751501; DOI=10.1021/bi00115a014;
RA Hammen P.K., Waygood E.B., Klevit R.E.;
RT "Reexamination of the secondary and tertiary structure of histidine-
RT containing protein from Escherichia coli by homonuclear and heteronuclear
RT NMR spectroscopy.";
RL Biochemistry 30:11842-11850(1991).
RN [17]
RP STRUCTURE BY NMR.
RX PubMed=1483471; DOI=10.1111/j.1432-1033.1992.tb17492.x;
RA van Nuland N.A.J., Groetzinger J., Dijkstra K., Scheek R.M.,
RA Robillard G.T.;
RT "Determination of the three-dimensional solution structure of the
RT histidine-containing phosphocarrier protein HPr from Escherichia coli using
RT multidimensional NMR spectroscopy.";
RL Eur. J. Biochem. 210:881-891(1992).
RN [18]
RP STRUCTURE BY NMR.
RX PubMed=8158637; DOI=10.1006/jmbi.1994.1254;
RA van Nuland N.A.J., Hangyi I.W., van Schaik R.C., Berendsen H.J.,
RA van Gunsteren W.F., Scheek R.M., Robillard G.T.;
RT "The high-resolution structure of the histidine-containing phosphocarrier
RT protein HPr from Escherichia coli determined by restrained molecular
RT dynamics from nuclear magnetic resonance nuclear Overhauser effect data.";
RL J. Mol. Biol. 237:544-559(1994).
RN [19]
RP STRUCTURE BY NMR.
RX PubMed=7853396; DOI=10.1006/jmbi.1994.0075;
RA van Nuland N.A.J., Boelens R., Scheek R.M., Robillard G.T.;
RT "High-resolution structure of the phosphorylated form of the histidine-
RT containing phosphocarrier protein HPr from Escherichia coli determined by
RT restrained molecular dynamics from NMR-NOE data.";
RL J. Mol. Biol. 246:180-193(1995).
RN [20]
RP STRUCTURE BY NMR.
RX PubMed=8868480; DOI=10.1002/pro.5560050305;
RA van Nuland N.A.J., Wiersma J.A., van der Spoel D., de Groot B.L.,
RA Scheek R.M., Robillard G.T.;
RT "Phosphorylation-induced torsion-angle strain in the active center of HPr,
RT detected by NMR and restrained molecular dynamics refinement.";
RL Protein Sci. 5:442-446(1996).
RN [21]
RP STRUCTURE BY NMR.
RX PubMed=10048929; DOI=10.1038/5854;
RA Garrett D.S., Seok Y.-J., Peterkofsky A., Gronenborn A.M., Clore G.M.;
RT "Solution structure of the 40,000 Mr phosphoryl transfer complex between
RT the N-terminal domain of enzyme I and HPr.";
RL Nat. Struct. Biol. 6:166-173(1999).
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 -!- INTERACTION:
CC P0AA04; P11989: bglG; NbExp=5; IntAct=EBI-902853, EBI-545674;
CC P0AA04; P08839: ptsI; NbExp=4; IntAct=EBI-902853, EBI-551533;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M10425; AAA24438.1; -; Genomic_DNA.
DR EMBL; J02796; AAA24440.1; -; Genomic_DNA.
DR EMBL; M21994; AAA24384.1; -; Genomic_DNA.
DR EMBL; M21451; AAA23655.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75468.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16289.1; -; Genomic_DNA.
DR PIR; A29785; WQECPH.
DR RefSeq; NP_416910.1; NC_000913.3.
DR RefSeq; WP_000487600.1; NZ_STEB01000039.1.
DR PDB; 1CM2; X-ray; 1.80 A; A=1-85.
DR PDB; 1CM3; X-ray; 1.60 A; A=1-85.
DR PDB; 1GGR; NMR; -; B=1-85.
DR PDB; 1HDN; NMR; -; A=1-85.
DR PDB; 1J6T; NMR; -; B=1-85.
DR PDB; 1OPD; X-ray; 1.50 A; A=1-85.
DR PDB; 1PFH; NMR; -; A=1-85.
DR PDB; 1POH; X-ray; 2.00 A; A=1-85.
DR PDB; 1VRC; NMR; -; C/D=1-85.
DR PDB; 2JEL; X-ray; 2.50 A; P=1-85.
DR PDB; 2LRK; NMR; -; D=1-85.
DR PDB; 2LRL; NMR; -; D=1-85.
DR PDB; 2XDF; NMR; -; C/D=1-85.
DR PDB; 3CCD; X-ray; 1.00 A; A/B=1-85.
DR PDB; 3EZA; NMR; -; B=1-85.
DR PDB; 3EZB; NMR; -; B=1-85.
DR PDB; 3EZE; NMR; -; B=1-85.
DR PDB; 4XWJ; X-ray; 2.10 A; B=1-85.
DR PDB; 5YA0; X-ray; 3.00 A; C/D=1-85.
DR PDB; 5YA1; X-ray; 2.70 A; C/D=1-85.
DR PDB; 5YA2; X-ray; 2.70 A; C/D=1-85.
DR PDB; 6KCR; X-ray; 3.50 A; B/D=1-85.
DR PDBsum; 1CM2; -.
DR PDBsum; 1CM3; -.
DR PDBsum; 1GGR; -.
DR PDBsum; 1HDN; -.
DR PDBsum; 1J6T; -.
DR PDBsum; 1OPD; -.
DR PDBsum; 1PFH; -.
DR PDBsum; 1POH; -.
DR PDBsum; 1VRC; -.
DR PDBsum; 2JEL; -.
DR PDBsum; 2LRK; -.
DR PDBsum; 2LRL; -.
DR PDBsum; 2XDF; -.
DR PDBsum; 3CCD; -.
DR PDBsum; 3EZA; -.
DR PDBsum; 3EZB; -.
DR PDBsum; 3EZE; -.
DR PDBsum; 4XWJ; -.
DR PDBsum; 5YA0; -.
DR PDBsum; 5YA1; -.
DR PDBsum; 5YA2; -.
DR PDBsum; 6KCR; -.
DR AlphaFoldDB; P0AA04; -.
DR BMRB; P0AA04; -.
DR SMR; P0AA04; -.
DR BioGRID; 4259700; 574.
DR BioGRID; 851226; 4.
DR DIP; DIP-35731N; -.
DR IntAct; P0AA04; 10.
DR MINT; P0AA04; -.
DR STRING; 511145.b2415; -.
DR TCDB; 8.A.8.1.1; the phosphotransferase system hpr (hpr) family.
DR SWISS-2DPAGE; P0AA04; -.
DR jPOST; P0AA04; -.
DR PaxDb; P0AA04; -.
DR PRIDE; P0AA04; -.
DR ABCD; P0AA04; 3 sequenced antibodies.
DR EnsemblBacteria; AAC75468; AAC75468; b2415.
DR EnsemblBacteria; BAA16289; BAA16289; BAA16289.
DR GeneID; 64724046; -.
DR GeneID; 67461150; -.
DR GeneID; 946886; -.
DR KEGG; ecj:JW2408; -.
DR KEGG; eco:b2415; -.
DR PATRIC; fig|1411691.4.peg.4316; -.
DR EchoBASE; EB0781; -.
DR eggNOG; COG1925; Bacteria.
DR HOGENOM; CLU_136230_2_3_6; -.
DR InParanoid; P0AA04; -.
DR OMA; APHGIHT; -.
DR PhylomeDB; P0AA04; -.
DR BioCyc; EcoCyc:PTSH-MON; -.
DR BioCyc; MetaCyc:PTSH-MON; -.
DR EvolutionaryTrace; P0AA04; -.
DR PRO; PR:P0AA04; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008047; F:enzyme activator activity; IDA:EcoliWiki.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:EcoCyc.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:EcoCyc.
DR GO; GO:0016775; F:phosphotransferase activity, nitrogenous group as acceptor; TAS:EcoCyc.
DR GO; GO:0033673; P:negative regulation of kinase activity; IDA:EcoCyc.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR GO; GO:0045819; P:positive regulation of glycogen catabolic process; IDA:EcoCyc.
DR GO; GO:0043609; P:regulation of carbon utilization; IDA:EcoCyc.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IDA:EcoCyc.
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;
KW Phosphotransferase system; Reference proteome; Sugar transport; Transport.
FT CHAIN 1..85
FT /note="Phosphocarrier protein HPr"
FT /id="PRO_0000107850"
FT DOMAIN 1..85
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 ECO:0000269|PubMed:2261470"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3CCD"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1HDN"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:3CCD"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3CCD"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3CCD"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:3CCD"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:3CCD"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:3CCD"
SQ SEQUENCE 85 AA; 9119 MW; E5C8879C0A95AD41 CRC64;
MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL QTLGLTQGTV
VTISAEGEDE QKAVEHLVKL MAELE
