ID A0A3S0JHT4_9PROT Unreviewed; 982 AA.
AC A0A3S0JHT4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EJ903_13330 {ECO:0000313|EMBL:RTR19472.1};
OS Azospirillum griseum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2496639 {ECO:0000313|EMBL:RTR19472.1, ECO:0000313|Proteomes:UP000277007};
RN [1] {ECO:0000313|EMBL:RTR19472.1, ECO:0000313|Proteomes:UP000277007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-25-5w-1 {ECO:0000313|EMBL:RTR19472.1,
RC ECO:0000313|Proteomes:UP000277007};
RA Yang Y.;
RL Submitted (DEC-2018) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:RTR19472.1}.
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DR EMBL; RXMA01000011; RTR19472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0JHT4; -.
DR OrthoDB; 7326651at2; -.
DR Proteomes; UP000277007; Unassembled WGS sequence.
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; cd00088; HPT; 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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
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; PS50894; HPT; 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:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000277007}.
FT DOMAIN 38..162
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 186..239
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 257..307
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 325..546
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 729..853
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 890..982
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 690..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..325
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 93
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 779
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 929
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 982 AA; 105031 MW; 2B4BBE2FD4C40C5F CRC64;
MSMGALADRM FDDDDILFAD EDDANGVGVA EEAPPPWTVL VVDDEADVHL MTNLLLADVT
FQNRPLDLIG AHTATHARMI LENRPDIAVI LLDVVMEQDD SGLRLVRWIR DDLGNRDVRI
ILRTGQPGQA PQRDVIVDYD INDYKPKADL SAESLFTAVI AALRAFDQIQ SIETRVAERT
RELRESREQI NAVLEASPIG VCAYDESGII VLTNHRLTTL LGVSKDRLLG GSIGELFAPM
EDRQDEQRWL FYRRQIRDAE VKLLRADGSS FWALMTVDPT HVNGQPVFLS WIYDITRRKL
AERQMENAKE QAEQATKAKS AFLATMSHEI RTPMNGVLGM LGLLERTELD SHQLDTVATM
RESATSLLRI IDDILDFSKI EAGKMDVERV VVSIPALVEG VAETLAPSAR AKGLSLLTYI
DPAIPPALLG DPVRLRQILF NLGGNAIKFT EHGRIVLRAG LSGLSPDSAA LRIEVIDTGI
GIPDAARRRL FQPFTQAESS TTRRFGGTGL GLSISRRLAT LMNGEIGVES NPGDGSTFWL
TLALDRVDAL PPVGDAPPVA DTPDDPMALD LSGLTVLLGV PDATERAFLS SYLEVAGARV
LPAGDPQQLA TQARIARDAG CPASVVAVDE ALRVPAAACA PEELGRRSGE ACPPIVLLMQ
GSGGDRPSGN TVPLGRPVRR VPFLRAVATA AGRGSSVEPP PTATTPSSRP AESVPVELDA
EQAHAEGRLI LVAEDNAVNR KVLGMQLRAL GYAAEMTPGG AEALAAWRGD RRYALLLTDV
QMPEIDGFEL TRRIRAAEQN GDGPAGAARL PIIAITANAA PGEVASYHAA GMDAVLSKPL
DLSQLAITLA RWMPPLSSDA PGVTVAAAPP PTNADAPIDL SALRALCGGD DGMVDELLGD
FRSTSREILA GLDAGLLNQD LSAVRAAAHN LKGSSRNAGA KPLADAALRL EQAANGTTDW
PTLTRLASDV HAAFAALEQH LS
//
