CRDS_HELPY
ID CRDS_HELPY Reviewed; 397 AA.
AC O25917;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Sensor histidine kinase CrdS {ECO:0000303|PubMed:15968080};
DE EC=2.7.13.3;
GN Name=crdS {ECO:0000303|PubMed:15968080}; OrderedLocusNames=HP_1364;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=12933888; DOI=10.1128/iai.71.9.5381-5385.2003;
RA Panthel K., Dietz P., Haas R., Beier D.;
RT "Two-component systems of Helicobacter pylori contribute to virulence in a
RT mouse infection model.";
RL Infect. Immun. 71:5381-5385(2003).
RN [3]
RP FUNCTION.
RX PubMed=15968080; DOI=10.1128/jb.187.13.4683-4688.2005;
RA Waidner B., Melchers K., Staehler F.N., Kist M., Bereswill S.;
RT "The Helicobacter pylori CrdRS two-component regulation system
RT (HP1364/HP1365) is required for copper-mediated induction of the copper
RT resistance determinant CrdA.";
RL J. Bacteriol. 187:4683-4688(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26082024; DOI=10.1111/mmi.13089;
RA Hung C.L., Cheng H.H., Hsieh W.C., Tsai Z.T., Tsai H.K., Chu C.H.,
RA Hsieh W.P., Chen Y.F., Tsou Y., Lai C.H., Wang W.C.;
RT "The CrdRS two-component system in Helicobacter pylori responds to
RT nitrosative stress.";
RL Mol. Microbiol. 97:1128-1141(2015).
CC -!- FUNCTION: Member of the two-component regulatory system CrdR/CrdS that
CC induces the transcriptional induction of the copper resistance
CC determinant CrdA in response to increasing concentrations of copper
CC ions (PubMed:15968080). Functions as a sensor protein kinase that
CC phosphorylates CrdR (Probable). In turn, CrdR functions as a
CC transcriptional regulator by direct binding to promoter regions of
CC target genes including the crdA promoter or nitric oxide-responsive
CC gene promoters (PubMed:26082024). {ECO:0000269|PubMed:15968080,
CC ECO:0000269|PubMed:26082024, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is not able to colonize the
CC stomach in mice (PubMed:12933888). It shows also a significant loss of
CC viability upon exposure to nitric oxide (PubMed:26082024).
CC {ECO:0000269|PubMed:12933888, ECO:0000269|PubMed:26082024}.
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DR EMBL; AE000511; AAD08404.1; -; Genomic_DNA.
DR PIR; D64690; D64690.
DR RefSeq; NP_208156.1; NC_000915.1.
DR RefSeq; WP_000951935.1; NC_018939.1.
DR AlphaFoldDB; O25917; -.
DR SMR; O25917; -.
DR STRING; 85962.C694_07040; -.
DR PaxDb; O25917; -.
DR EnsemblBacteria; AAD08404; AAD08404; HP_1364.
DR KEGG; hpy:HP_1364; -.
DR PATRIC; fig|85962.47.peg.1461; -.
DR eggNOG; COG0642; Bacteria.
DR OMA; FSEMIDY; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
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 Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW Kinase; Membrane; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..397
FT /note="Sensor histidine kinase CrdS"
FT /id="PRO_0000448702"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 197..395
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 200
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 397 AA; 45852 MW; 1D0CA359F99D227A CRC64;
MAIALTHYEK KSLKLFLGIY LGSSFVLMLV ISVLAFNYEK NEKIKMIRMD MDKMASKIAS
EVIALHMQTH GDYQNALNAL ISRYKDASIA LFDSKKRVLY SNIPESANLI KNHKEAGFFS
FRGEYYLLSD ETFAHLGVAK MLFKNSKPLH FSSLYRNIVL VFVVAFLCVI GVSVFLGRLF
LKPIRNEITR IDHFLKNTTH ELNTPMSALV LSLKTLEDNQ QHRRIKIAIQ RMSFLYRSLS
YLVMQDIERE SFVLLDLKAL IIKENTLFSE MIDYHKLEFK SDLVEVELKA KEQDFISLYS
NLLMNAIKYS VMNGYIHIEL THAFLKVKNL GYEIPKDKIT ELSVRYVRFN SGVLGYGIGL
GLVKKVCEKY KMRLEIHSEP SLKGSFYENS FCVQFQG
