ID K0C417_CYCSP Unreviewed; 926 AA.
AC K0C417;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Q91_0451 {ECO:0000313|EMBL:AFT66491.1};
OS Cycloclasticus sp. (strain P1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT66491.1, ECO:0000313|Proteomes:UP000006282};
RN [1] {ECO:0000313|EMBL:AFT66491.1, ECO:0000313|Proteomes:UP000006282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:AFT66491.1,
RC ECO:0000313|Proteomes:UP000006282};
RX PubMed=23144416; DOI=10.1128/JB.01837-12;
RA Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus
RT sp. strain P1.";
RL J. Bacteriol. 194:6677-6677(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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003230; AFT66491.1; -; Genomic_DNA.
DR AlphaFoldDB; K0C417; -.
DR STRING; 385025.Q91_0451; -.
DR KEGG; cyq:Q91_0451; -.
DR PATRIC; fig|385025.3.peg.463; -.
DR HOGENOM; CLU_317073_0_0_6; -.
DR Proteomes; UP000006282; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 6.10.340.10; -; 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; IPR033479; dCache_1.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFT66491.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006282};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 297..350
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 359..412
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 436..486
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 680..917
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 646..673
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 926 AA; 103513 MW; 3A99693C43ECEAEF CRC64;
MFSVAALMSL SLLLMGGSIY FSSMHLAEKQ ALGLLLEQQE DYSDEITSVL KNSKSNLLTF
AEIPAVEATL RTNQDGGIEP VSTEGAKVCA SGLNQVVRAF LANYPNYLSL TLLNAEGKVL
AGALHLAADQ EVMRLADKAV YYSDIKHQQA DGLPILTVST PIYINGQVEG VAVAEISALP
LLNSAIEKRK GIDTYIIDNK GKFWVGPNEI TDFSAYFLAN ERQQNEYVLI NEKRNSVLAV
HKILFDEKNS QRYWGVIHEL PKSVVFKHLD QARDSMLITG LMIVLLAVFF ASMLVSRIII
NPIVRLVEGC RAVGDRNFSV RLDETSVDDE FKELFQAFNE YTEQSEVILK EMKKQADSSA
KSLENVVVHM EDALIMMDEF GTIKSCNPAV IDLFGYDEKE MVGNNINLLI PELFKEEHEK
SDADYKGTGA SKGIEHNGEV VGRRKSGSVF PMGLSINEYR VNEEQHFIGI FRDITVRKAM
ELEIQQTDER LKKQYNSYLS LSDFVRRAST NFEEACNKIL QECAEVLQAD WVGLWLFNNK
RDALLCQNYY SGREKSYFTL PSLLVSEHEY YFSELLMEGG LLSNETTPLL SHFPEQAHSP
VSTLQLPVTK YKSIAGVFNV VNQDEARVLR SDEAQYVKSL SMLVEVLLEE ESRRRVQEQL
KETNKELALA SQMKSQFLSN MSHELRTPLN AIIGFSELLK GGVLGPLTEE QSQYSKEIFD
SGSHLLDLIN GILDLSKIEA GKEQLALDEV SIQSLLQSTV YMLRDKANAR GISITEEVEE
KVTVCLLDER KTKQIVINLL SNAVKFTPKG GSIVISATID KVLHPDFRLD DSELAQCETP
YLKLSVSDTG IGISEENIGK LFRRFEQIDG SLAREFEGTG LGLSLVKAMT ELHGGFVTVV
STLGEGSTFS VYLPYKKVDL ETDYLV
//