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Database: UniProt
Entry: Q4KAU3_PSEF5
LinkDB: Q4KAU3_PSEF5
Original site: Q4KAU3_PSEF5 
ID   Q4KAU3_PSEF5            Unreviewed;       642 AA.
AC   Q4KAU3;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=PFL_3537 {ECO:0000313|EMBL:AAY92804.1};
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY92804.1, ECO:0000313|Proteomes:UP000008540};
RN   [1] {ECO:0000313|EMBL:AAY92804.1, ECO:0000313|Proteomes:UP000008540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC   {ECO:0000313|Proteomes:UP000008540};
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY92804.1; -; Genomic_DNA.
DR   RefSeq; WP_011061816.1; NC_004129.6.
DR   AlphaFoldDB; Q4KAU3; -.
DR   STRING; 220664.PFL_3537; -.
DR   KEGG; pfl:PFL_3537; -.
DR   PATRIC; fig|220664.5.peg.3614; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_51_6; -.
DR   Proteomes; UP000008540; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
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; 2.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AAY92804.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AAY92804.1}.
FT   DOMAIN          12..70
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          87..139
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          140..213
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          209..267
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          287..503
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          525..636
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         575
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   642 AA;  70400 MW;  1D9990F70B06447A CRC64;
     MPDLPEPYHP LTDDRFRLLV DAVVDYAIYM LDAQGRVASW NSGARRFKGY REEEVLGRHF
     SCFYTPEDRQ AGLPQRALDS AAQCGRFEGE GWRLRKDGTR FWCHVVIDPI RDSAGGLIGF
     AKVTRDMTEQ RAAEQILKQS EQQFRLLVQS VTDYAIYMLD AQGRVSSWNL GAQRIKGYAP
     EEVIGQHFSL FYTAEDRASD EPRKALEAAA REGRFEKQGW RLRKDGTRFL AHVIVDPIRA
     DSGAIIGFAK ITRDITEVVQ AQKELEVARE ALFQSQKLQA IGQLSGGIAH DFNNLLTVIR
     GNLELLHKRV GDDPRLRRLL DNALQGTERG VTLTQRMLAF ARRQELKSQA LDLGQLVASL
     SGLLCSSVGP RIALRVEMAP DLPAVQADLN QLELALLNLV SNARDAMPEG GSILIEAQLR
     GATGNLARGQ YVCLAVVDDG QGMDEQTLAC AADPFFTTKG LGKGTGLGLS MVHGLAEQLG
     GRLVLQSRLG QGTRAELWLP LASAAKGSPG SEAMPAPGPD HPPLCVLLVD DDSLVLDSTT
     LLLEDLGHRV IRAASGAQAL QCLEQHRDIQ LMISDMAMPH MDGRQLAEAV RRLHPQLPII
     LASGYAQRQD GPVPELPRIF KPFSQAQLRD ALAQVLAQSA AG
//
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