ID A0A0G3BSY7_9BURK Unreviewed; 950 AA.
AC A0A0G3BSY7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, 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=AAW51_2954 {ECO:0000313|EMBL:AKJ29645.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ29645.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ29645.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ29645.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-2015) 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; CP011371; AKJ29645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3BSY7; -.
DR STRING; 413882.AAW51_2954; -.
DR KEGG; pbh:AAW51_2954; -.
DR PATRIC; fig|413882.6.peg.3084; -.
DR Proteomes; UP000035352; 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; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
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; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
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; 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; PS50112; PAS; 2.
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:UP000035352};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 250..302
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 312..382
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 451..500
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 501..555
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 575..799
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 822..938
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 287..315
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 873
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 950 AA; 104036 MW; 8339343CD277A474 CRC64;
MEDGHADPGG LGRGPAIGAN DLPAGPDFGP VARLAATLCD TPSALITVHD GQAPRVVATA
GLDAIAVAAG ALVLQCEPLS GEATQVVEDL RADRRYAGAP CVLAPPHLRF YACVPLRSPS
GLTLGTLAVL DCVPRQLRVD QIQALETAGH LLAVEIELRR RWQAQLCERA DTMRRTNSLL
AMAGRLAHVG GWELDLASGH AQWSDQVAAI HGVPAGETLE VSAALALYVD ESRERLKAAF
DRCAATGASY DEEVELCALD GQRRYVRSIG HAVKDATGAV VGVQGVLQDI TERRLAEQQQ
QQQQQQQQQQ RLSSRLAETL ESITDAFCCV DPDWRLVVVN REFERLLELS RDECLGGVVW
DLFPDSLGST FEMEARKAVK DHRATDFETY YEPLKRWFEV RLFPSPEGLA IYFRDVSERH
ARLEQLRLLD IGIGHSNDVL MITDARLEPP GPRIVYVNQA VERLCDYHRS EVLGRSPRML
QGPKTRRSEL ERISAALHAK HSVRAELINY GKTGREYWVE LEISPICDRD GRCTNFVAVE
RDITLRKQED ERRRELEDQL RQAKKMESVG TLAGGIAHEF NNILAAILGN LQLAQEDLPD
RAAALEHLAH IRQSSQRARS LVQHLLAFGG RQSSERRQQD IRAVMDETLV LLRHTLPDTI
NLQVSVSAAP LFAALDGNQL QQALLSLCTN ARQALPDEQG VITIGLEDVT LEQADVSRLG
LLAPGCHAHL WVSDTGNGID ESTRARIFDP FFTTRPPGQG TGLGLAVVHR IVMAHDGAVA
VESTPGQGST FHLYIPALRD AGDEDAPTRP GALDALHGAG QHVLYVDDDE MMLLTVEALL
QRLGYHVTCY ADPHVAVAAL TSQARRCDLL LTDQNMPGLT GIELARQVLQ LHPELPVIII
TGFLTDELRH EALQAGVRDI IPKQNCVEEL GGAVARTLAA STSAPQLPSH
//
