ID A0A1X7H2V1_9PROT Unreviewed; 862 AA.
AC A0A1X7H2V1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02982917_4850 {ECO:0000313|EMBL:SMF78813.1};
OS Azospirillum oryzae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=286727 {ECO:0000313|EMBL:SMF78813.1, ECO:0000313|Proteomes:UP000192936};
RN [1] {ECO:0000313|EMBL:SMF78813.1, ECO:0000313|Proteomes:UP000192936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2P {ECO:0000313|EMBL:SMF78813.1,
RC ECO:0000313|Proteomes:UP000192936};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FXAK01000007; SMF78813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7H2V1; -.
DR STRING; 286727.SAMN02982917_4850; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000192936; Unassembled WGS sequence.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 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; 3.30.450.20; PAS domain; 3.
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; 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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF13426; PAS_9; 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; 2.
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; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 171..223
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 434..484
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 497..724
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 744..860
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 795
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 862 AA; 92007 MW; 07956A34546466A2 CRC64;
MDVADTDRPL RPAGAAEPVS GSSRLSASFP GALAALTGVG TLLGLSASGQ IGFPAAAALA
AAGGLALWSA VRAGSAAAAL ARSNAALVRT RDDLEGLRAR SRDFAAVSPG WFWETGSDHR
YLSLSGGLTD LLGCDPRTVF GDSLFDLGPL VADEATWAEY RADIESGRPF RDLEVSFEGV
DGRDLVLRLS AVPVRGSDGR FRGYRGCGVD ATAETLALVE ARFMQAVVHD AIDSVSEGFV
LFSADGRLLI CNEQYRRAYP TIADMLTPGR SFAEILRAAA ERGGLEGADD IGAWVEQRLT
RHLQHSAPVD GRLSDGRWYR ISEHATGTGG VVKILMDITE LKTREQELAD QTARLKQTVA
ALRESELRYR QLVELAPYGI VIWDRAAIRF ANGAAAAILG MAADVLEGQP LAGFLEDGDA
LAATLATAAD GEEQRLECDA LRPDGERRRL EVAASQAVYA GGPAVLLVLN DITDRRRVEG
ELQRAQKMEA VGRMAGGIAH EFNNMLTAIG GFARLAERNP ADPDRVLTCV QEIAKASERA
AALTGQLLDF SHRRVTDERE VVAVAPLVRD LRVFLKPLLS AGIDVAILAE DEGAHVLVNP
VTLNQALLNL ALNGRDAMPH GGTLTIALTT EVPDDAFFAR HRSLKPGRYV VIRVTDQGTG
IPPEIRDRIW EPFFTTKEPG KGTGLGLWMV YGTAQQSGGA VELEDAAAEA GHGTSFALYL
PAVDTPAEPA GLDPLHVAEG EGAVILLVDD EDSVRRYLRL VLEEAGCTVV EASDGQEALI
RYDEAGGLFD AVVSDVSMPR MNGLELARAL EARNQLLPIL FLTGYASRET AAGLTAQEGR
QIVMKPVTPE RLLAALRDLL AL
//
