ID A0A1X7ID95_9BACT Unreviewed; 1255 AA.
AC A0A1X7ID95;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05661096_00532 {ECO:0000313|EMBL:SMG12654.1};
OS Marivirga sericea.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX NCBI_TaxID=1028 {ECO:0000313|EMBL:SMG12654.1, ECO:0000313|Proteomes:UP000193804};
RN [1] {ECO:0000313|EMBL:SMG12654.1, ECO:0000313|Proteomes:UP000193804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4125 {ECO:0000313|EMBL:SMG12654.1,
RC ECO:0000313|Proteomes:UP000193804};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FXAW01000001; SMG12654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7ID95; -.
DR STRING; 1028.SAMN05661096_00532; -.
DR OrthoDB; 5522855at2; -.
DR Proteomes; UP000193804; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 7.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 7.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 6.
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; PF08447; PAS_3; 3.
DR Pfam; PF13426; PAS_9; 4.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 7.
DR SMART; SM00091; PAS; 7.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 7.
DR PROSITE; PS50112; PAS; 6.
PE 4: Predicted;
FT DOMAIN 131..204
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 208..261
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 255..303
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 330..384
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 381..425
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 454..507
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 504..548
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 576..630
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 631..703
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 708..761
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 762..807
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 842..894
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 972..1023
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1041..1254
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1255 AA; 144282 MW; 8F7B30664046FC51 CRC64;
MKNLQGILYN CVRQNELFFQ MIQNDAVEGY IFWERGEQQN LLLDSKLSQQ LELKTLTDLD
KLKASKGEFL HSIIEKVENQ LGDEFSENDI FNTSVFQPVN NTDIRFSTCQ SKESNALYIL
AAIQRTTYFN RNRSITDISN VLEVAVWQYN VFSGEVLINE MWASLIGYSK KELYPVTVKT
FEDLTHPQDF EEFKTVLQKY IDGESKSYTM EIRMRHKEGY WKWVLAKGKI VTRNEDGEVE
WMMGSHIDIT KRKIRENQME ILAQVPISTN NAVIISDANG KITFVNNAFE EITGYLLEEV
LGKKPGDFLQ GPLTDQKDIA SFRKHLSLGR SFTQEILNYS KTGDPYLLSC QVDPIFNDKG
EISKFISLQR IITEEKKNKE FLATFKNTLD QTEDCIFIFD QEDLKFTYVN QGAINMMGYT
EEEMLLLHPY DLKPEFPKVE FQALIKPLAE DRIPSIRFQT IHRAKNGRDI PVEVFLQFIK
NEKVSPHFVA VVKDITDQLA IEKELSRLSL VAKKTTNLVV ITDNIGKIEY VNPAFEQKTG
YKLEEVIGSK PGKFLHGKET KSEHIKATRA GLKTLKPFTQ EILNYSRSGE KYWVSITFNP
VFNESGELTN FIAIESDITE QKHKETLLRE SEERLQFVLE GSELGYWDIN LETGKTTMND
RYFELLGYTA ENFEQSIHFY QSLVHPDDIG KLTRLMDTSF IPGGQDDFSM ELRVKHKLGH
YVWILDRGAV VKRDEKGTPL RISGTHTEFS RRKKLEIELQ EERDFFSRVI GSNTLSLVIV
AKSGKITFAN RGAEKVLGII KSEIEDKVYD DPDWRHITLE DEPFDIEKLP FPIVMHTKKS
VQDIRHGIEW ADGTKKYLSI SGGPFNLEDG EIQDVIFSVA DITERVKTQK QLDLAKDQMQ
SILKDMSDVV WSVDLPDYKM KFITPSIEKL TGFPASYYLE NYQGNRWEER VYDADRGLVT
QAYEDLDKNG SYEIEYRIRT KDNLLKWVLN KGTIIYKNGL PSRLDGYITD ITNRKKQENS
LAKYLGIVED QNERLKNFTY IVSHNLRSHS ANIQGLVYLI NKKNPKIAEN EYVKMLSKAS
NKLDETLHHL NNVVSVVSST EEMEKINLSD AIATFLDAFE NVISEAQLYF LNEISNNVVI
EAVPAFLESI ITNLLTNAIK YCDSQKDFSF VRISNRSLNG IVIMEVQDNG LGIDMEKYGE
KLFGMYKTFH THTDSRGLGL FLTKNQVESI GGKITVESKL GVGTTFKVFL KDGSI
//
