ID Q9I2B7_PSEAE Unreviewed; 564 AA.
AC Q9I2B7;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=ercS {ECO:0000313|EMBL:AAG05380.1};
GN OrderedLocusNames=PA1992 {ECO:0000313|EMBL:AAG05380.1};
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:AAG05380.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG05380.1, 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).
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};
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DR EMBL; AE004091; AAG05380.1; -; Genomic_DNA.
DR PIR; H83397; H83397.
DR RefSeq; NP_250682.1; NC_002516.2.
DR RefSeq; WP_003106469.1; NZ_QZGE01000026.1.
DR AlphaFoldDB; Q9I2B7; -.
DR SMR; Q9I2B7; -.
DR STRING; 208964.PA1992; -.
DR PaxDb; 208964-PA1992; -.
DR GeneID; 880217; -.
DR KEGG; pae:PA1992; -.
DR PATRIC; fig|208964.12.peg.2076; -.
DR PseudoCAP; PA1992; -.
DR HOGENOM; CLU_000445_114_75_6; -.
DR InParanoid; Q9I2B7; -.
DR OrthoDB; 9764438at2; -.
DR PhylomeDB; Q9I2B7; -.
DR BioCyc; PAER208964:G1FZ6-2030-MONOMER; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; NF041832; near_NosP_CTERM; 1.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002438}.
FT DOMAIN 117..166
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 209..422
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 446..561
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 157..202
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 495
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 564 AA; 62338 MW; F1FD019688C11477 CRC64;
MARPSEQQQE ALAGLLGLGS HSARKSHYPE LLARLEELEA ERNRYKWLFE HAVHGIFQAS
LGQGLRAANP ALAQMLGYDD PQQVLWSLED MAGQLFVGGE AEMRRIRALL RERGGLFGYE
TRLWRRDGSH IEVLMNLLLR HDEEELVEGF VADITERVQA QQRLQTMNEE LERRVAERTH
ELEELNRQLR QARDAAEAAN HSKDKYLAAA SHDLLQPLNA ARLLVDTLRE RGLPAAELQL
VERTHLALEG AETLLTDLLE IARLDQSAIR PDLDDYSLDE LLAPLASEFE EVARAAGLAL
RARIPRLAVR TDARLLSRIL RNLLSNACRY TERGSVLLGA RRRGGKVRLE VWDTGRGIPA
DQLQAIFLEF NQLDAGRASE RRGVGLGLAI VDRIAGILGY RIEVHSTPGR GSLFAIEVPL
VRKPARPAPG EAIARVSAGD PLPGRRLLVV DNETEILFSM SALLGQWGCE VLTATDLEGA
RKALDGRAPD AILVDYHLDH GATGCQLLGA LREDYGAEIA AVMITADRSD DCRRALARLG
VPLLNKPLKP GKLRAALSAL LGEL
//