HPRS_ECOLI
ID HPRS_ECOLI Reviewed; 452 AA.
AC P76339;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Sensor histidine kinase HprS {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000305|PubMed:15522865};
DE AltName: Full=Hydrogen peroxide response sensor {ECO:0000303|PubMed:27983483};
GN Name=hprS {ECO:0000303|PubMed:27983483}; Synonyms=yedV;
GN OrderedLocusNames=b1968, JW1951;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AUTOPHOSPHORYLATION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15522865; DOI=10.1074/jbc.m410104200;
RA Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.;
RT "Functional characterization in vitro of all two-component signal
RT transduction systems from Escherichia coli.";
RL J. Biol. Chem. 280:1448-1456(2005).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION, AND INTERPLAY BETWEEN HPRSR AND CUSSR.
RX PubMed=25568260; DOI=10.1099/mic.0.000026;
RA Urano H., Umezawa Y., Yamamoto K., Ishihama A., Ogasawara H.;
RT "Cooperative regulation of the common target genes between H(2)O(2)-sensing
RT YedVW and Cu2+-sensing CusSR in Escherichia coli.";
RL Microbiology 161:729-738(2015).
RN [7]
RP FUNCTION, INTERPLAY BETWEEN HPRSR AND CUSSR, AND MUTAGENESIS OF CYS-165;
RP CYS-333 AND CYS-338.
RX PubMed=27983483; DOI=10.1099/mic.0.000410;
RA Urano H., Yoshida M., Ogawa A., Yamamoto K., Ishihama A., Ogasawara H.;
RT "Cross-regulation between two common ancestral response regulators, HprR
RT and CusR, in Escherichia coli.";
RL Microbiology 163:243-252(2017).
CC -!- FUNCTION: Member of a two-component regulatory system HprR/HprS
CC involved in response to hydrogen peroxide (PubMed:25568260,
CC PubMed:27983483). Senses H(2)O(2), maybe via the redox state of the
CC membrane (PubMed:27983483). Activates HprR by phosphorylation
CC (PubMed:15522865). Can also phosphorylate CusR (PubMed:15522865).
CC {ECO:0000269|PubMed:15522865, ECO:0000269|PubMed:25568260,
CC ECO:0000269|PubMed:27983483}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:15522865};
CC -!- INTERACTION:
CC P76339; Q46896: ygbT; NbExp=3; IntAct=EBI-554869, EBI-1130209;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15522865}.
CC -!- MISCELLANEOUS: HprSR and CusSR form a unique regulation system, where
CC both two-component systems recognize and regulate the same set of
CC genes, but under different environmental conditions. HprSR plays a role
CC in H(2)O(2) response regulation, while CusSR plays a role in Cu(2+)
CC response regulation. {ECO:0000269|PubMed:25568260,
CC ECO:0000269|PubMed:27983483}.
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DR EMBL; U00096; AAC75034.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15795.1; -; Genomic_DNA.
DR PIR; D64961; D64961.
DR RefSeq; NP_416477.1; NC_000913.3.
DR RefSeq; WP_000826792.1; NZ_LN832404.1.
DR AlphaFoldDB; P76339; -.
DR SMR; P76339; -.
DR BioGRID; 4259161; 16.
DR BioGRID; 850838; 1.
DR DIP; DIP-11852N; -.
DR IntAct; P76339; 4.
DR STRING; 511145.b1968; -.
DR PaxDb; P76339; -.
DR PRIDE; P76339; -.
DR EnsemblBacteria; AAC75034; AAC75034; b1968.
DR EnsemblBacteria; BAA15795; BAA15795; BAA15795.
DR GeneID; 946487; -.
DR KEGG; ecj:JW1951; -.
DR KEGG; eco:b1968; -.
DR PATRIC; fig|1411691.4.peg.282; -.
DR EchoBASE; EB3797; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_6_6; -.
DR InParanoid; P76339; -.
DR OMA; DIAMGHE; -.
DR PhylomeDB; P76339; -.
DR BioCyc; EcoCyc:G7056-MON; -.
DR BioCyc; MetaCyc:G7056-MON; -.
DR PRO; PR:P76339; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IDA:EcoCyc.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0046688; P:response to copper ion; IEP:EcoCyc.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR006290; CztS_silS_copS.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR01386; cztS_silS_copS; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..452
FT /note="Sensor histidine kinase HprS"
FT /id="PRO_0000074914"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..158
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 181..234
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 242..452
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT SITE 165
FT /note="Essential for the response to H(2)O(2)"
FT /evidence="ECO:0000269|PubMed:27983483"
FT MOD_RES 245
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MUTAGEN 165
FT /note="C->A: Loss of H(2)O(2)-dependent transcription of
FT hiuH."
FT /evidence="ECO:0000269|PubMed:27983483"
FT MUTAGEN 333
FT /note="C->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:27983483"
FT MUTAGEN 338
FT /note="C->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:27983483"
SQ SEQUENCE 452 AA; 50850 MW; 172A6410C3CEBE8A CRC64;
MKRLSITVRL TLLFILLLSV AGAGIVWTLY NGLASELKWR DDTTLINRTA QIKQLLIDGV
NPDTLPVYFN RMMDVSQDIL IIHGDSINKI VNRTNVSDGM LNNIPASETI SAAGIYRSII
NDTEIDALRI NIDEVSPSLT VTVAKLASAR HNMLEQYKIN SIIICIVAIV LCSVLSPLLI
RTGLREIKKL SGVTEALNYN DSREPVEVSA LPRELKPLGQ ALNKMHHALV KDFERLSQFA
DDLAHELRTP INALLGQNQV TLSQTRSIAE YQKTIAGNIE ELENISRLTE NILFLARADK
NNVLVKLDSL SLNKEVENLL DYLEYLSDEK EICFKVECNQ QIFADKILLQ RMLSNLIVNA
IRYSPEKSRI HITSFLDTNS YLNIDIASPG TKINEPEKLF RRFWRGDNSR HSVGQGLGLS
LVKAIAELHG GSATYHYLNK HNVFRITLPQ RN
