ID H0PV55_9RHOO Unreviewed; 1031 AA.
AC H0PV55;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AZKH_2093 {ECO:0000313|EMBL:BAL24406.1};
OS Azoarcus sp. KH32C.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL24406.1, ECO:0000313|Proteomes:UP000007106};
RN [1] {ECO:0000313|EMBL:BAL24406.1, ECO:0000313|Proteomes:UP000007106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH32C {ECO:0000313|EMBL:BAL24406.1,
RC ECO:0000313|Proteomes:UP000007106};
RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA Senoo K.;
RT "Complete genome sequence of Azoarcus sp. KH32C.";
RL Submitted (NOV-2011) 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; AP012304; BAL24406.1; -; Genomic_DNA.
DR RefSeq; WP_015435711.1; NC_020516.1.
DR AlphaFoldDB; H0PV55; -.
DR STRING; 748247.AZKH_2093; -.
DR KEGG; aza:AZKH_2093; -.
DR PATRIC; fig|748247.4.peg.2056; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_282088_0_0_4; -.
DR OrthoDB; 9152656at2; -.
DR Proteomes; UP000007106; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 2.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
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; SM00091; PAS; 2.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 499..544
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 571..621
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 657..874
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 902..1019
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 605..647
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 952
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1031 AA; 113134 MW; BA9E5FF2D7BD1452 CRC64;
MSTPHRDPPP ATKRARAARA RRATLRATRP SPILLPRRVD DTLLRVLDSL PAIIYVSDMQ
SHEIIFANRY THEALQTDKL VGRVCWQAIQ VGQTGPCEFC TNPRLVDEHG SPAEPHVWEF
RNTLNGRWYH IYDRAIEWLD GRIVRLEIAT DITQRVTAET RLQRLTMIYA ALNRCNQEIF
RCNSEDELFP RVCRAAVELG GMRAAWVGLV DPDTGILNPI AAFGTGAEEQ ILQEPLPISA
SAPLGRAPTS TAIRLGHPVW CQDFLADERT ASWHEEARRH GWAAAGALPI VRDGKVIGNF
TLYAGETDAF DEAAQNLLVE LASRLGIALE KIAREHDRKH SENALRFVAE ELSVESGSSF
FQALAIRLAK LLDADFALVG ELDAEGETVS TIGLVTPDGV ANNFRYELPG TPCADTVATG
CSIHRSTVAT LFPDDLHLIE MEAQAYVGVP LRDEAGDTIG LIAALWRRPL TPDEHPEHVM
RIFSARAAAE LVRSRTETAL QLTRFSLEAA TDGLFWINCD ARFVDVNSAA CQLLGYDRAE
LLQRGIADVD VRYSTDGWSR FSDRLTKRGS ISFESMLRHR DGHLIPVEVV AGHVKIGNRE
LNCSFVRDIS ERKRAKEALE RLNEELEERV AQRTEELLAA KEEAERANLS KSEFLSSMSH
ELRTPLNAIL GFSQLLKADP AAPLTTDQGE SLDEILRAGK HLLALINEVL DLARIESGRL
ELAPESVELA PLAQECLSLV RPLAEARRIA LGAEVPTDCL LRVDRLRLRQ LLLNLLSNAV
KYNRDGGEVS LVATTEPGLV HLAVHDTGIG IAPEFLPRLF KPFERHGEAS RQVEGTGIGL
ALCKRLVEAM GGTIAVDSRP GEGSVFRVTI PCTPTPAACA SPAAAHEPET AASPDAAGAT
HTLLYVEDNA ANLRLVQKII ALHPRLRLID AVTAETGLEL ARACHPDLIL MDLGLPGICG
MEALRRLRQI PGLRDTPVIA LSANAMPDDI TSARAAGFDD YLTKPLDVAR FQALLKSYLQ
GSAINPLSSR A
//
