ID A6GYD8_FLAPJ Unreviewed; 870 AA.
AC A6GYD8;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=FP1017 {ECO:0000313|EMBL:CAL43111.1};
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612 {ECO:0000313|EMBL:CAL43111.1, ECO:0000313|Proteomes:UP000006394};
RN [1] {ECO:0000313|EMBL:CAL43111.1, ECO:0000313|Proteomes:UP000006394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86
RC {ECO:0000313|Proteomes:UP000006394};
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL43111.1; -; Genomic_DNA.
DR RefSeq; WP_011963162.1; NC_009613.3.
DR RefSeq; YP_001295922.1; NC_009613.3.
DR AlphaFoldDB; A6GYD8; -.
DR STRING; 402612.FP1017; -.
DR EnsemblBacteria; CAL43111; CAL43111; FP1017.
DR GeneID; 66552414; -.
DR KEGG; fps:FP1017; -.
DR PATRIC; fig|402612.5.peg.1030; -.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_114_71_10; -.
DR OrthoDB; 9781208at2; -.
DR Proteomes; UP000006394; Chromosome.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
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; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR011645; HNOB_dom_associated.
DR InterPro; IPR042463; HNOB_dom_associated_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 NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF07701; HNOBA; 2.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CAL43111.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006394};
KW Transferase {ECO:0000313|EMBL:CAL43111.1}.
FT DOMAIN 269..317
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 341..395
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 396..466
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 469..521
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 518..563
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 590..644
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 662..870
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 128..165
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 870 AA; 99812 MW; D58389231F6D75EC CRC64;
MNTLEFNFNE DSFNKLFPFY ILIDTNLKIK SFGKSLAKIC PNIKKSLSFK NNFEVVRPHL
DNLNFNELAS NCNQLIIIKY INSNTPIRGQ FELINNSLLF VGSPWFGSMS DVIEKKLTLH
DFAIHDPLLD LLHILNNQEN TANELKELLT TINDQKNKLK QANKEIHDIA LFPTQNPDPI
IRIDTKGNLL KRNPAAEKLS SFIYDEINYK IEDFFKFIIT KIDPEKERWI FEIQNDQKYY
SFVCISLKED NYINIYGRDI TQQKKTEEES NRLSLVASAN QNGVVFTNPN GIIFWCNNAY
LKLTGFSREE VIGKTPIEIG KTNHTNKSDL KKMIEPFYKG IPFDIDLIHA RKDGSSFWSK
NKGQPILNSK GEVIQYFAMI EDISLKKRYD ESLQNEKEKY RSIIANMNLG LLEVDLNDVI
TLANNSFLTI SGYSSEELIG KKAAELLLTQ ESKKLVKSKN EIRKKGKTDS YEVKVIDKFG
KNRHWLISGA PNYNAMGELI GTIGIHLDIT LQKEQEEKLY LLSLIAEKNI NSVIIANPEG
KIEWANKSFI EISGYTIEEL IGKRPGNLLQ GKETNPETII YLRDQIKKGL PFNCEIINYS
KQGKKYWINI QGQALYNKKG QIVKFFAIEE NITKKKELEE KQDFLVKSLA KSNKELEDYA
SIVSHDLKSP LRSIHSLISW IKEDNDNQLN DQTLQYLSLI EGKVEKMDYL IEGILTYAKI
DKINLASEKV NTHEIIENII NIIHIPNHIN VSIIGKLPII NADKFRIQQL FQNIISNAVN
YIDKPIGTVN VSCIEKDGKY IFSIQDNGPG IAKENQEKIF KIFQSLQKSD KSTGLGLSIV
KKIIETYNGK IWLESQINHG TTFFISLNDQ
//
