ID W8Q865_9PSED Unreviewed; 795 AA.
AC W8Q865;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CD58_05270 {ECO:0000313|EMBL:AHL32335.1};
OS Pseudomonas brassicacearum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=930166 {ECO:0000313|EMBL:AHL32335.1, ECO:0000313|Proteomes:UP000019521};
RN [1] {ECO:0000313|EMBL:AHL32335.1, ECO:0000313|Proteomes:UP000019521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF41 {ECO:0000313|EMBL:AHL32335.1,
RC ECO:0000313|Proteomes:UP000019521};
RX PubMed=24812222;
RA Loewen P.C., Switala J., Fernando W.G., de Kievit T.;
RT "Genome Sequence of Pseudomonas brassicacearum DF41.";
RL Genome Announc. 2:e00390-14(2014).
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; CP007410; AHL32335.1; -; Genomic_DNA.
DR RefSeq; WP_025211979.1; NZ_CP007410.1.
DR AlphaFoldDB; W8Q865; -.
DR KEGG; pbc:CD58_05270; -.
DR PATRIC; fig|930166.5.peg.1022; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000019521; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AHL32335.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:AHL32335.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..795
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004911861"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 429..644
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 668..782
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 377..404
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 717
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 795 AA; 88824 MW; F075ECEAB2AD6E5F CRC64;
MRLLQFLLLA IALLSTGLLH AAPVDICRAD HLDLMPAIQI FEDTQASLSL EDVARLPETR
FNAATPGWPT QGYSRSAFWL KVQLTNSSAV ACSRLLVIGA PRLEDIRVYQ SGHDAHAGAA
YPLAEWPQPA ARQPAFPVAL AAGQSVTVFV RVASHFQMLL EPELWSEPAL LRSQQQTYLS
DGLTLGIVLL VVPFGFIVGW ILRSRLLSVN AGAVLSYILL TCILNGYLIY WPAALGWTRE
LLTFASAVSF VLFLAYFRVL LQVSVLPKVI GWSYWLPLSG CVLGRLWWLK VDPVQGAQIV
QISLLSFYGV LLVTLFMAWR RRLSYSWLAW LVSGLLLAQL LMRMLFPQEQ LPWQSPQSKY
SLSSTLPGVM LLVCTLIMEV ARSRNREKNA LSTLEQQRQA EHERLESTVA LRTAQLRESL
AARSALMARI SHDLRSPLVR IIDYARLLHA GPNRDYQATI ERNARQQLEL IDEMLEFSRG
ELEQMQLTLA PGYLYGFLKE VVDEAGFLAA RQGNTFEAVL ADDLPPLVEA DFKRLRQVLM
NLLANAAKFT RNGQIRFAVS AAPGAAADTV ELRFSVIDSG IGIDPQEFEQ LLQPFHRGRN
AQRYEGSGLG LSIVTQLLER MDSRLEPQAT EQGSHFSFRL QLKCAEEHDL ENGIVDNNAT
PFDGTGQHVL LVDDIEQNSE WLYDLLAGYG FDVSMAANGE DALACLAQQP VDLLISDQMM
PGMDGWELLL QVRERWRDLP VMLYSAVPAR RPKGYPQDLA FDAVLLKPAD SSELLARVKT
LVCSDTVPRA MAWER
//
