ID A0A1S1J5Y6_9FLAO Unreviewed; 1350 AA.
AC A0A1S1J5Y6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BHE19_09195 {ECO:0000313|EMBL:OHT44885.1};
OS Flavobacterium tructae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1114873 {ECO:0000313|EMBL:OHT44885.1, ECO:0000313|Proteomes:UP000180252};
RN [1] {ECO:0000313|Proteomes:UP000180252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSU {ECO:0000313|Proteomes:UP000180252};
RA Chen S., Walker E.;
RL Submitted (SEP-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHT44885.1}.
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DR EMBL; MIKE01000023; OHT44885.1; -; Genomic_DNA.
DR RefSeq; WP_070907238.1; NZ_MUHH01000038.1.
DR STRING; 1278819.BHE19_09195; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000180252; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OHT44885.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 243..317
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 353..423
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 427..479
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 831..905
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 908..959
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 976..1198
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1231..1349
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1282
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1350 AA; 156156 MW; CBFE3BC56F9F512B CRC64;
MVANYSLFNS LIPGVAILGN ALKSIITKWY VINSDIIFYN NPKLIMLGLS MIAFLTLLVY
QFFRIKTRIG YFIERKPETE TVNREYHLYI LFFGIALIVI EIINEIFKIR PKSLLLVNVS
IGFSMLLFYF IIGKIKFLKE RVQSIFILSF FVYLFYIGYN IIYRTNDIIP IIAFLIFFYF
SYSILKPIKL YWFFVGLVFT FLITTVVYQL IPVKSSIILI NYCVLIFILN QVKYAVLLNN
SDNFRFTNEI VHKGNSLTIA TNEKNEILFC SETITSILGY LPDEVMGAKF WKLTNETDYP
ENLSNINHEE DKLYIRKLRS KNGEYKYIQW KDKRFSQGLI ISIGQDVTEQ ITVRDQYKNL
IQTATDIIFE IDSDGYFTFI NDFGFSILGY SENEIISQHY SNFIHENYQR NAVDFYENLE
MNENNFPTIE IPILKKNGKK LWISQKIIVR KNDLGQTIGF AGIARDITEI RNIENDKRKR
LKKIESYNNS INKLSTTDFS QYDNLNTVID FIIKEAAIVT KTNRVSFWKC HKDLISCKNL
FSIDKQHLND KNILDKQSYP IYFETLKSKA IINAPDVFNK LETSEFQKLY FTKNHIKSML
DVPIFLNGQL VGVVCFESTE EKRNWDNEDI NYARTISDVI SLAISSQMRL EAEKKLEFKS
QLLSALSLCT EKFLMSKSTQ EMFQETYNLI GKAAKVDHMY YYEKDFTTNT VSQKYKWSRQ
GIEHQITKLQ RLTKDQLQEI YDAAQNKKIV NTLTRKLDNT FFKQLLIANE IKSILILPLY
INDIFTGFIG FDDCTKERKW SEEEIYIFQV LANNISSALE RNRNETKILE SEEKFKLIAN
NIPGTVYLSK FDAFSTKIFL NDEILNLTGY SKSEFIENNL SFLSLIHPDD KDEVINNQID
NLQSGMPLHN IYRIRRKTGE FIWVEEFGDV IKKGDEIEFV GGIYFDITNK KESEDAIKAK
QLAEAANKSK SDFLANMSHE IRTPLNGIIG FTHLLMNTGL EEIQEKYMTT INQSAHSLLD
IINDILDFSK IEAGKLELFI DLYDIKKVLG QVFDLIVYES NQKNLQLELN VAPDVPKYIW
TDIVRIKQIL INLLSNAVKF TNKGSIKLNV SVLEKSSNND CTIRFSVVDT GIGILEKNQK
KIFKAFSQED SSTTRKFGGT GLGLTISNQL LALMESRLQL ESKIDKGSNF YFDLNLKTSN
QSISEKYNTE LQNTSLELNS DDPVSNQKSI TFLIVEDNKV NMLLLKTIIK NLYSGAYIHE
CENGYEAVSQ FENINPDLVF MDIQMPIMNG YETTRAIRNT IIGKDIPIIA VTAGAEKEER
NKCLSAGMND YISKPIMKGS VEEALVKWLK
//
