ID F0GCF3_9BURK Unreviewed; 1219 AA.
AC F0GCF3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B1M_29625 {ECO:0000313|EMBL:EGD00827.1};
OS Burkholderia sp. TJI49.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=987057 {ECO:0000313|EMBL:EGD00827.1, ECO:0000313|Proteomes:UP000003049};
RN [1] {ECO:0000313|EMBL:EGD00827.1, ECO:0000313|Proteomes:UP000003049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TJI49 {ECO:0000313|EMBL:EGD00827.1,
RC ECO:0000313|Proteomes:UP000003049};
RX PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT isolated from dieback affected mango orchards.";
RL World J. Microbiol. Biotechnol. 29:2033-2044(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGD00827.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEXE01001813; EGD00827.1; -; Genomic_DNA.
DR AlphaFoldDB; F0GCF3; -.
DR PATRIC; fig|987057.7.peg.4641; -.
DR BioCyc; BSP987057:G10O5-1293-MONOMER; -.
DR Proteomes; UP000003049; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000313|EMBL:EGD00827.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:EGD00827.1}.
FT DOMAIN 6..193
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 216..450
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 854..1077
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1100..1217
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 622..723
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 45
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1149
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1219 AA; 131548 MW; CDC2277C2F4CA9BE CRC64;
MGSNFTTEQL RVVVLGGSAG SLDALRAIVA ALPAQAGFAV LVITHLDPSE ESRLADILQA
DSRMPVEKLA HLRKIEHDRL YVLPENAGVI ALDGHFRLTR RQAGLNLPID TCLASLAQDP
DVNGAAVILS GTGQDGASGL VDLKASGGFA IAQQPQTASH QGMPTAAIDT GLVDEVLPPA
DIARCLVQRF GDPARGDGTA DGQASDHDAL GTAVSIVQQK TGINLGYVKD VNLRRRFLRR
VLLQKDRDVD AYLQLLRSDA REAEALRDDI LIGVTAFFRD AEFVNVLRQS VIPSLLELKR
DPIRVWVPAC STGEEVYTIA TLLREALDRE ALHRHVQIFG TDINEASIEI ARAGRYSLAS
IDDVPEAFRE TTFAATSGGY VVRKSIRDMC VFARHNVLTH APFSGMDLIS CRNLLIYLRK
EAQQHVLEVL HYACRPDGFV LLGRAEAVSG TDGFEHAGAP HLYRKVPAAK RQQGAFPIDA
LRPWASQGVA PSVRRVQQPD PVLEAANRAA LERYAPPGFV VDDKGDVVHF RGDVSGFVAP
ASGEASLALP RLLRPELNVT VRTALIEAKR TGHPVRRERV ALDDAYFALE VLPLAADDLV
PHYLVTVERL PADAPAPQSA GAGSANGRVQ ELERTITTLS DELEATQGQL KSVVAEFESA
NEELRTANEE MLSTNEELQS ANEELLLAKQ ELESANQELA SLNEELKSRN QQLDRANDDL
SNLVEGIPLP VVVLDRQLRL RHFSPQAQTL FALPDDSVGQ PMAQQNKLFS AADLERVVQS
AVQGLADVEH EYQDSEGRWW LVNVRAYRTA DDRIDGAVLA FQDIDALKRA LGTAQAARTE
AERANTAKDN FLGLVSHELR APLNVISGWA AVLATASERG MPADEQMSQR AVTTIMRHCQ
LQAELIDDLL DVSRISSGRF SLDTKPADFA AIVQTVVESN RPVAARKEIS LATAGLNARA
VVSGDARRLQ QVASNLIGNA LKFTPQGGRV EVALTRLGTM LELSVTDNGI GVSAEQLPYL
FDRFMQSDTS RTRNYGGLGL GLSIVKHLVT AHGGTVTASS EGEGRGTRLT VRLPSLQDSI
VDADAAAPAS SGSVRLEGLS VLLVDDDVQA QEALAHLLRG LGAQVQLATG AKDALARLAA
GSFDILISDL AMPDDDGHAL LRGVREREGD RQRIYALALT GLASINDRDA AIAAGFDDHL
PKPVNLQLLL EKLSLGRGR
//
