ID A0A0K1QX11_PSEFL Unreviewed; 1377 AA.
AC A0A0K1QX11;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B723_29355 {ECO:0000313|EMBL:AKV10286.1};
OS Pseudomonas fluorescens NCIMB 11764.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1221522 {ECO:0000313|EMBL:AKV10286.1, ECO:0000313|Proteomes:UP000017175};
RN [1] {ECO:0000313|EMBL:AKV10286.1, ECO:0000313|Proteomes:UP000017175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11764 {ECO:0000313|EMBL:AKV10286.1,
RC ECO:0000313|Proteomes:UP000017175};
RX PubMed=23144379; DOI=10.1128/JB.01670-12;
RA Vilo C.A., Benedik M.J., Kunz D.A., Dong Q.;
RT "Draft genome sequence of the cyanide-utilizing bacterium Pseudomonas
RT fluorescens strain NCIMB 11764.";
RL J. Bacteriol. 194:6618-6619(2012).
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; CP010945; AKV10286.1; -; Genomic_DNA.
DR RefSeq; WP_017340209.1; NZ_CP010945.1.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000017175; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17580; REC_2_DhkD-like; 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; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
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; IPR013767; PAS_fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 19..204
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 228..514
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 823..873
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 874..931
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1017..1236
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1258..1374
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 666..735
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 32
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 59
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1307
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1377 AA; 153952 MW; 9499AA1068ACF811 CRC64;
MTTTPNRPAS HKEQKASRPS TLDFPVVGIG ASAGGLQAIK LFFENMPQDN GMAFVIILHL
SPDHQSIADR IIQESTRMPV LQVSKTVSIE KNHVYVISPA QRLSMNDGLL EVSACETRES
RHASIDLFFR DLANVHRERA FCVVLSGTGS DGAVGLSRIK EQGGVTLAQA PQDAEFDGMP
RAAIDTGMVD LVLPVVEMPQ KLLELWRNSQ EISLPTANDP ELQTIAAVSE REALIAEQLL
HDVLIQLRTG TGHDFKHYKR ATVLRRIERR MQVTAQPDLA AYYRYLQDNP EETKALLGDM
LIGVTNFFRD REAFEALERD VVPQLVSAAV SAHPEKEEIR VWSAGCSTGE EAYSLAMLLS
DQLQLDASAA SMQLFATDID ERAISVGRAG LYPQAIVTDV PPTRLRHYFL KEDDHYRIRK
EIREKVLFAK HSLLSDPPFS QIDLIVCRNL LIYLDREVQR EILQMFHFAL RPGGFLFLGS
SESADACHEL FAPVDKRNRI FRAKTGTANS RRTPTMPRGG YVRTNISQQP AQNSVQRKLS
FADIHQRALE QSAPPSVIVD ANADILHMSE SAGRFLRHVG GELSRNLLTL ILPDLRLELR
TTLFQVQQSA LPVKSREVPI KRDDRRHLIN LVAHPYKDEG SDSEYVLVIF EEVEVDPSEL
AATTVLQNEN QVLSNLEREL QRTKLHLQDT IEQSEVSSEE LKASNEEMQA INEELRSATE
ELETSKEELQ SINEELLTVN FELKTKVEET DKINDYLTNL IASTDIATVF VDRAMRIKWF
TPRATDIFSM LPVDTGRSLL DITHRLDYDN LASDATQVFE SLKMIEREVS STDNRWYIAR
LLPYRSSEDH IDGTVLTFID ITKRRAAEEE LRQGEERMRL VAESTRDYAI ITLDEQGVIT
SWNKGAELIF GYSKAEAEGA YYDFIFSPED RAAGVPENEL LAVRTHGRSE DERWHQHKDG
SRFFCSGEVT LLRGDNLQGY VKIARDLTGH KRQHEAQSQE LAETRNTNYL KDEFFAVMSH
ELKHPLNLIQ LNAELLRRLP VTKSLAPAAK AVNTICDAVT SQARIIDDLL DVARVRTGKL
KLQPVAVDLA SVLRDVHTVV LNDQHDVTVE LLVPSDALMV QADPTRLEQI IWNLVNNALK
FTPPKGRVQL IASQSGDMAR LDIKDNGAGI APENLEHVFD LFSQAEKQHI THNREGLGIG
LSLVRQLTEA QHGSVEVSSG GSGTGCTFTV YLPLARAHGE VQPAACAEDV SGRLSGLTIL
LVDDSADVLE TLKMLLEMED AQVIAFDRPV AALDAAKSTR FDLIISDLGM PVMNGHELMS
ALRQLPLAKD VPAIALTGYG ANSDIQKSRQ SGFDQHIGKP VSYDDLISTI ETLRRQR
//
