ID A0A1D7QC19_9SPHI Unreviewed; 1364 AA.
AC A0A1D7QC19;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BFS30_03015 {ECO:0000313|EMBL:AOM76221.1};
OS Pedobacter steynii.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=430522 {ECO:0000313|EMBL:AOM76221.1, ECO:0000313|Proteomes:UP000094313};
RN [1] {ECO:0000313|EMBL:AOM76221.1, ECO:0000313|Proteomes:UP000094313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DX4 {ECO:0000313|EMBL:AOM76221.1,
RC ECO:0000313|Proteomes:UP000094313};
RA Seilhamer J.J.;
RL Submitted (AUG-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; CP017141; AOM76221.1; -; Genomic_DNA.
DR RefSeq; WP_069377917.1; NZ_CP017141.1.
DR KEGG; psty:BFS30_03015; -.
DR OrthoDB; 9809670at2; -.
DR Proteomes; UP000094313; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 8.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000094313};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 804..826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 847..1068
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1112..1227
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1259..1358
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1160
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1364 AA; 155085 MW; 3FB560318A20F6EF CRC64;
MRFIKRSFSL PLLSFLIFLQ VITYAQQDIR FSNLSLENGL SQNSVMAITQ DHQQFVWFGT
KHGLNRYDGY EFKVYKNNPN DPKSISSDEI TSILTDHEGV LWVGTVKGLN RYDSKNDAFI
QITANPKVKN SISSNAIEHI YQDTQKNLWI GTLRGVNLLS DRKKNEFKTF LFKDVSTNRG
INSIYATLSD NNNHIWLATS DGLIRMNIKN GHYHIYRHDQ RKTGSLSSNY ITSLARDAEQ
NLWIGTDNGL NLFHPADTSF SVYQHSKNSN SLVHNDIREV MPDRKGMLWI GTQEGLSIFD
PRTRKFINYR HDPELKESLS HNSIHSIFQD RNNSIWIGTF YGGVNIVHPF PTAFHAYKNS
KLRPSISSNI VSSIVEDQRN NLWIGTEGGG LNYYNRNDHT YTYYKISLNH KQGLTSNLIK
TICKDRNGNL LIGTHHGGLN LFNPTTGTFR SVVNVKDDNQ TISTAEIIAI CEDRARNIWV
GSYSGLNLLK MTDGVPAATT VKSPLEKKLQ NKRIQFLFED REQNLWIGTQ GGLHVYNPDT
KEFRYFLKDK NNRDKLQSDY INCIIQTAAG DLGIGTYFGG LSIYNPRTKK FKTYTEKEGL
SNNNVLGIIE DDAHNLWIST DNGLSKLDPR TGKFQIYTKS DGLAGNDFNV RSYFKDSKGE
LFFGGYNGLT SFYAEQIAVN RNPSPVVFTG LKLFNRPVAV NGPDQLLKED LISSKRITFA
YDQNHFTIGF ALLNYIKSDK NRYAYKLSDY DKDWNYTNEP SATYSNLPSG QYTFLVKGVN
NDGIAGAAPV KIEIRIKPPI WASWWAYCIY LLIFAAILFL TIRYLVIRAV LKRSVDLQQM
KLSFFTNISH EIRTPLTLIL GPLENLLKST QDNIELNRQV IPIKNNADRL MRLITELMDF
RKMEAGHMKL NVHEGDIVTF SKEIFLAFSQ MALHRNIHYN FECQQESITL YFDKDQLEKV
LFNLLSNAFK FTPDEGKITL SIQEFTDFAE IKVLDNGKGI PYESQNKLFS DFFQVDEHGS
SHIGSGIGLA LSKSIVSSHY GKIEIQSHPA TAEKAGDTCF TVTLKKGKAH FKPAELMEAI
AYELPSENHF PAPVRLPSAA VETSTPNTPS ETILIVEDNP EIRTLISSLL NNQYQIEESE
DGLKGWEKAI ETLPDLVICD IMMPVMDGLE LCRKLKEDER TSHIPVILLT ARSTHIHQVS
GMETGADAYI TKPFSTALLE LNIRNLINSR AAMRRRYGQQ VTLQPQNVVI GSTDQAFISR
VLKYIEENMA DQSFGVPDLA SEIGMSQPVL YKKIRAITDL SVNDFIKSIR LKKAAQLLEQ
NVYTISEISY LIGFNDPKYF SREFRKQYGE TPRGFINKLK ENHS
//