ID Q9I0V9_PSEAE Unreviewed; 472 AA.
AC Q9I0V9;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=Sensor protein {ECO:0000256|RuleBase:RU364088};
DE EC=2.7.13.3 {ECO:0000256|RuleBase:RU364088};
GN OrderedLocusNames=PA2524 {ECO:0000313|EMBL:AAG05912.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG05912.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG05912.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007829|PDB:5GPO}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 40-165 IN COMPLEX WITH ZN(2+).
RX PubMed=28732057; DOI=10.1371/journal.ppat.1006533;
RA Wang D., Chen W., Huang S., He Y., Liu X., Hu Q., Wei T., Sang H., Gan J.,
RA Chen H.;
RT "Structural basis of Zn(II) induced metal detoxification and antibiotic
RT resistance by histidine kinase CzcS in Pseudomonas aeruginosa.";
RL PLoS Pathog. 13:e1006533-e1006533(2017).
CC -!- FUNCTION: Member of a two-component regulatory system.
CC {ECO:0000256|RuleBase:RU364088}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085,
CC ECO:0000256|RuleBase:RU364088};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU364088}.
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DR EMBL; AE004091; AAG05912.1; -; Genomic_DNA.
DR PIR; A83331; A83331.
DR RefSeq; NP_251214.1; NC_002516.2.
DR RefSeq; WP_003113318.1; NZ_QZGE01000008.1.
DR PDB; 5GPO; X-ray; 1.70 A; A/B=40-165.
DR PDBsum; 5GPO; -.
DR AlphaFoldDB; Q9I0V9; -.
DR SMR; Q9I0V9; -.
DR STRING; 208964.PA2524; -.
DR PaxDb; 208964-PA2524; -.
DR GeneID; 878718; -.
DR KEGG; pae:PA2524; -.
DR PATRIC; fig|208964.12.peg.2638; -.
DR PseudoCAP; PA2524; -.
DR HOGENOM; CLU_000445_89_6_6; -.
DR InParanoid; Q9I0V9; -.
DR OrthoDB; 5561773at2; -.
DR PhylomeDB; Q9I0V9; -.
DR BioCyc; PAER208964:G1FZ6-2559-MONOMER; -.
DR BRENDA; 2.7.13.3; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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 NCBIfam; TIGR01386; cztS_silS_copS; 1.
DR PANTHER; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5GPO};
KW ATP-binding {ECO:0000256|RuleBase:RU364088};
KW Cell inner membrane {ECO:0000256|RuleBase:RU364088};
KW Cell membrane {ECO:0000256|RuleBase:RU364088};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364088};
KW Membrane {ECO:0000256|RuleBase:RU364088};
KW Metal-binding {ECO:0007829|PDB:5GPO};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364088};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002438};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364088};
KW Transmembrane {ECO:0000256|RuleBase:RU364088};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364088};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|RuleBase:RU364088}; Zinc {ECO:0007829|PDB:5GPO}.
FT TRANSMEM 171..194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364088"
FT DOMAIN 195..248
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 256..470
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5GPO"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5GPO"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5GPO"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5GPO"
SQ SEQUENCE 472 AA; 51878 MW; EFE439A9030A1606 CRC64;
MTPPGRLSLR LALLVGALGA LLALALGAMA HWNLGRELEA RERENLQLKL EQIRHSLEDD
LDLRSDPAVQ AHALQDQLVA HSGLHLSILD SRSGQPLMSF GDQAAASVAA NRALLARLQA
DARQPVFQSW STGNDQRLLS IGASMRMKNG TPVQVLLSSE RNADERLLDG FLRATLLALP
FLLPLIALAA WWVVRAGLEP LNRFRRVAAQ VSPQDLSYRI PEQNLPRELD SLARSFNHML
GRLEDGVRQL SQFSDDLAHE LRAPICNLLV RNQVLLSQHR DGAAYREALE SNAEELERLS
RIVTDMLFLV QVDNPAIQAQ FGCVALHEQA AKVIDLYEMV AEDKGVELRL SGNGFAHGDN
LMIQRAISNL VSNAVRHTPQ GGRIDVRIGE RAGHTEVRVS NDGPGIPPEY LPHLFERFYR
RAGRQTGAQA GTGLGLAIVQ SIMAYHGGRA EAESVPQQKT HLRLLFPSTG AA
//
