ID A0A126ZAX9_9BURK Unreviewed; 1163 AA.
AC A0A126ZAX9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AX767_03975 {ECO:0000313|EMBL:AMM23595.1};
OS Variovorax sp. PAMC 28711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM23595.1, ECO:0000313|Proteomes:UP000070169};
RN [1] {ECO:0000313|EMBL:AMM23595.1, ECO:0000313|Proteomes:UP000070169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM23595.1,
RC ECO:0000313|Proteomes:UP000070169};
RA Park H.;
RT "Complete genome of Variovorax sp.";
RL Submitted (FEB-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};
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DR EMBL; CP014517; AMM23595.1; -; Genomic_DNA.
DR RefSeq; WP_068628823.1; NZ_CP014517.1.
DR AlphaFoldDB; A0A126ZAX9; -.
DR STRING; 1795631.AX767_03975; -.
DR KEGG; vaa:AX767_03975; -.
DR OrthoDB; 9796305at2; -.
DR Proteomes; UP000070169; Chromosome.
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 CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AMM23595.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000070169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 493..713
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 772..885
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 894..1010
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1040..1157
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 721..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 389..483
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 821
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 943
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1090
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1163 AA; 127361 MW; EFEC48AEDA124C12 CRC64;
MKSQPAIDPQ AFQRVLSRNV KLPLVAGVLG AAVFVGLIFY LLSVIGWVEH TDQVTRNATE
AQRLSVDMES SMRGYLISGD VRFLDPYQSA QSRIDGELGA LRALVADNKA QVARVDRIAA
AQTSWDAYAA DLIALRRADQ DYRQSVNAGR GKALSDAMRS DYATFLNIEQ NLRFQRNNDA
NRTSLLVVGA YVLFSLLLTG ALGYFGRRQL AQLSGSYEAA LAEQTAHSEV LQQQAWLRSA
QNELAGELVG QLSVQELGRK TLAFFGRHIG SNVGALYLRE PQGQLRRAAA YGFSAAAEAS
PQIFSGTQGL LGQAATERRT VLVEPVEADY LKVNSGLGET APRAALLLPV THEGQVNGVI
ELGLMRAPNE RATTLLDTVA GTIGSAVAGS RYREQLQDVL AETQQLNEEL QVQQEELRTA
NEELEEQSRV LRQSQATLEN QQAELEQTNS QLSERTDALD QRNAALKRVQ LDLEDRAEEL
QRASRYKSEF LANMSHELRT PLNSALILSK LLGDNPQGNL TPEQVKFAES IYSSGNDLLV
LINDILDIAK VEAGKLEVQP EVVAVNSVAE SLRMTFTPLA NDKKLAFELD VAPDAPVSLV
TDRQRVEQIL KNLLSNALKF TDRGTVRLHV SARAGGGAQF AVSDSGIGIA VDQQDVIFEA
FRQADGTTSR RYGGTGLGLS ISRDLTRLLG GELQVHSVPG QGSTFTLALP ADIAQPLTAA
ERSDGAATAP QPRPLRATGM PAAKPAASPL VPAPDIPQFA DDRALPPDLS RRVLVIEDEP
QFAHILYDLA HELGYRCLVA HGAADGFALA RQYVPDAILL DMRLPDSPGL GVLQHLKDDS
HTRHIPVHVV SAQDQSEAAL HMGAIGYALK PASRDQLKDV FAKLEQKLSQ KVKQVLVVED
DALQRDSVIH LIADDDVAIT AVGTGEEALA LLRTRVFDCM ITDLKLPDLQ GSELLQRMAL
EDIVSFPPVI VYTGRNLTRA EEAELLRYSR SIIIKGARSP ERLLDEVTLF LHKVESELSS
ERQTMLKTAR GRDRVFEGRR ILLVDDDVRN IFALTSALEQ RGAVVEVGRN GIEALAKLDE
VPDIDLVLMD VMMPEMDGLE ATRRLRQDAR FQKLPVIAVT AKAMKDDQEQ CLAAGANDYL
AKPVDLDRLF SLLRVWMPKM ERL
//
