ID A0A2S2CW41_9PROT Unreviewed; 1035 AA.
AC A0A2S2CW41;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-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=DEW08_20825 {ECO:0000313|EMBL:AWK88507.1};
OS Azospirillum thermophilum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2202148 {ECO:0000313|EMBL:AWK88507.1, ECO:0000313|Proteomes:UP000245629};
RN [1] {ECO:0000313|Proteomes:UP000245629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFH 70021 {ECO:0000313|Proteomes:UP000245629};
RA Zhao Z.;
RT "Azospirillum thermophila sp. nov., a novel isolated from hot spring.";
RL Submitted (MAY-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}.
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DR EMBL; CP029354; AWK88507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2CW41; -.
DR KEGG; azz:DEW08_20825; -.
DR OrthoDB; 7991996at2; -.
DR Proteomes; UP000245629; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.58.920; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; 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 InterPro; IPR038188; TorS_sensor_sf.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AWK88507.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000245629};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 318..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..390
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 412..633
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 665..783
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 845..946
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 790..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 378..412
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 716
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 884
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1035 AA; 108965 MW; 704B6FA4BA59C55A CRC64;
MRGWLARKAR GSPRGLPIRG GVSRRMGLGL SLMVAVLLAV SGAAIYDLAQ FRQALSTLSN
GALPRITTGA VVTGGLQQVL AQATRLGAAA SHPERRVTLD ALMRELDAVV LSARDLSDID
GSATLAGVLS TLTLTVKDLD GLVARRIDAA ARADAALDEA RRLSAEADRL VAAVLPTLPP
EHLGALAAWT TEVNRVLTES THAGSSRYQR EILRVEKEAA AVLAALPARY AALPPEQAAR
FAGLNRRLEA ALLGRDGLLP SLVERQTATA RSKALTQQVV VMVEEVVKIA RSLFERINAT
AAGEAANLSA MAARQTSVLI GLGGLGFLIA AGVYLYLRGF VTLRLVRLNG AVLDRVEGRQ
TPLPEDGSDE ISTIARSIRH FLDEIARRQQ QVEEARERAE EASRAKSDFL ANMSHEIRTP
MNAILGLSHL ALRGDMPPAQ RAYLGQIRTS ATTLLGIIND ILDVSKIEAG MLTLEQVPFD
LSAVLGNLAT VAGLSARDKG LDLRIDVGPD VPAALTGDPL RLGQVLLNLV NNAIKFTQQG
GVTVAVGMAR SGEGEAELAF AVRDTGIGMT AEQIGRLFQP FSQADSSTTR RYGGTGLGLA
ISRRLTRMMG GDIAVESRPG EGSVFRFTVS VGVRDGGTVA AVTAGEPAPV PAGDLRVAEP
LRGQRVLVAD DNAINRQVAR ELLEDAGLVV TVVASGEEAV RRALAPGAGY GVLLTDIQMP
GMDGYQVARE VRRHLGPDRL PIIAMTAHAL EEERRRCLEA GMDDHIAKPV EPRRLVALLD
RWLKPCAAPL PGDGSAATDR QADAPAAAAL PPGLPPGLPP EVPAELPAEL DGFQLGPALA
RMNGHGRTLR VAIVDFHDRY RDGAATLRRM LAAGDWQGME RFVHGLRGSA GTVGAMAVFE
AAGLLERALR QGRRDALPDR LAALADALVP ALAAAATLVP RPAAAPAAAP PARKLAPSDL
RALEPLVLAL DEALRLGSMK AVDRVAALLA GLEGSRQEAA AAAIERSVDA LDFAEARAAL
ARLAAELEIA LEPAA
//
