ID A0A024HMV1_PSEKB Unreviewed; 782 AA.
AC A0A024HMV1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-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=PKB_4856 {ECO:0000313|EMBL:CDF86176.1};
OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF86176.1, ECO:0000313|Proteomes:UP000025241};
RN [1] {ECO:0000313|EMBL:CDF86176.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF86176.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Linke B.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDF86176.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF86176.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA Roy S., Van der Meer J.R.;
RT "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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; HG322950; CDF86176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024HMV1; -.
DR STRING; 1301098.PKB_4856; -.
DR KEGG; pkc:PKB_4856; -.
DR PATRIC; fig|1301098.3.peg.4843; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_69_6; -.
DR OMA; RPDYPPF; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000025241; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR Gene3D; 1.10.287.130; -; 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 Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CDF86176.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000025241};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:CDF86176.1}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..782
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001530109"
FT DOMAIN 312..382
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 385..437
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 455..676
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 782 AA; 87251 MW; A1F3C5CA5A4E339B CRC64;
MPCRRLLAAC LMSLALLCSL AHASLVALSA DERAWLDAHQ TLRVGLYGGG WPPFEMLDNE
GHFEGLSADY LNQVAQRLGL RLQPVLLDDW QAVLEAARKG EIDLLPTVAR TEERERFLAF
TRPYLSTSSL IFARRDSNVR VLDDLSGKRV AVERDFAVHD LLRAAVPGVS FVFTDDSAAA
LKAVSAGQAD AYIGNLISTT YLLSQLNLSN LEVRGDSGLD NSQVRFAVRK ELQPLVPLID
RALSSIDDDE RQRIHDKWLP SSNPFDWQQL LQAAWPYVAG FFALLTFVLI WNRRLQIQVA
ERARAEAEEH RQRKTLMALI DSIPDPIWFK DIQGRYLGVN QAFAECLGLR AEDVVGRSDE
QLFSDQSRAG RRDRDRQALS AREPFASEGW VVYPDGRRVL FDTLRSAFHD DHGELLGLVG
VSRDITARKA TEDALGQARD LAEQAARLKS EFLANMSHEI RTPLNIIIGL SHLLEATALD
PQQRDYLGKI QGSGQYLLEL ISDILDLSKV EAGRLEFERI EFDFERLLGE LVDLFAIRAA
GKGLTLHCEL DPKLPARLIG DPLRLRQILM NYGNNALKFT ERGELGLDVR VDMEAGDEVW
IYFGVSDTGI GLEPAQQERL FESFSQADNS ITRRYGGSGL GLAICKRLAE AMGGEVGVSS
EAGKGSLFWC RLPLGRVDDA PRLDPQQVQR ERPVAPPPLA VEASVPAAPV DDQEVEQVVR
RLAHLLAADD PRAGRLLGER ASLLRSVFNE GYDSLAASVR RFEFERALEN LLMLARERHI
RI
//