ID A0A1M7NB13_9FLAO Unreviewed; 807 AA.
AC A0A1M7NB13;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216269_11082 {ECO:0000313|EMBL:SHN00370.1};
OS Flavobacterium xinjiangense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=178356 {ECO:0000313|EMBL:SHN00370.1, ECO:0000313|Proteomes:UP000184092};
RN [1] {ECO:0000313|EMBL:SHN00370.1, ECO:0000313|Proteomes:UP000184092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.2749 {ECO:0000313|EMBL:SHN00370.1,
RC ECO:0000313|Proteomes:UP000184092};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRCL01000010; SHN00370.1; -; Genomic_DNA.
DR RefSeq; WP_073209936.1; NZ_FRCL01000010.1.
DR AlphaFoldDB; A0A1M7NB13; -.
DR STRING; 178356.SAMN05216269_11082; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000184092; Unassembled WGS sequence.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 8..126
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 162..219
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 226..278
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 310..531
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 553..668
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 125..152
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 602
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 807 AA; 90135 MW; 88089BD1DCCD3B69 CRC64;
MKINSPVKIL LVDDLPENLF ALEVILSTED YICVKATSGN DALKILLHEQ DFAIILIDVQ
MPLMDGFETV ELIRQIETLK HVPIIFLTAS MDNTVQIFKG YQAGAVDYMI KPLSPEILKA
KVAVFVDLYK KNQELLAQAE ELKKLNNELT AQKLLSEYSL SLIEASHDPL FAISPEGKIT
DMNNASVQVT GIQREKLIGT DFFDYFTEPQ KAREVYQKVF KKGFVADSPL ILRHKNGKLT
DVLFNGSVYK DEKGNVLGVV IVARDVTDQK RIETELIEAK VFAELATLIA EEAKSKAEDA
MKAKQQFLSN MSHEIRTPMN AIIGFTKVLI KTHLTEKQNE YFNAIKVSGD ALIVLIDDIL
DLAKVDSGKM TYEQTPFKIA TSLSAMLHLF ETKIHEKNLQ LIKNYDSKIP EVLVGDPVRL
HQIILNLVSN ALKFTTKGEI TVGVELVHED NETVIIRFAV TDTGIGIAAE KMPTVFENFQ
QATSGTSRLY GGTGLGLAIV KQLVETQGGS IQVESKIDQG STFSFTLPFR KTKAKAKSQT
VATQLNSEIK NIKVLVVEDI ALNQLLMKTL LDDFGFERDI AENGKIAIEL FQENSYDIIL
MDLQMPVMNG FEATDYIRNT LKSKIPIIAL TADVTTIDLA KCKAVGMDDY ISKPVDEKIL
YSKIVGLVKK PNLEKTEEFI AIENSQRKKT KCIDLTYLNN RTKSNPALMM EMITLYLTHT
PPLITTLKQS LEDKNWTLLA AAAHKIIPSF AIMGISANFE SMAKKIQELA DKEENTTELI
DLISQLEAIC AQACEELEEE FANIKSK
//
