ID K0NGV2_DESTT Unreviewed; 603 AA.
AC K0NGV2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=zraS {ECO:0000313|EMBL:CCK79063.1};
GN OrderedLocusNames=TOL2_C08950 {ECO:0000313|EMBL:CCK79063.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79063.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK79063.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(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};
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DR EMBL; FO203503; CCK79063.1; -; Genomic_DNA.
DR AlphaFoldDB; K0NGV2; -.
DR STRING; 651182.TOL2_C08950; -.
DR KEGG; dto:TOL2_C08950; -.
DR PATRIC; fig|651182.5.peg.1075; -.
DR HOGENOM; CLU_000445_89_29_7; -.
DR OrthoDB; 9773941at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0005886; C:plasma 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:CCK79063.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Transferase {ECO:0000313|EMBL:CCK79063.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 329..381
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 394..603
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 603 AA; 68960 MW; 3950EDFC1E27BB93 CRC64;
MKKHAVFFVS PLLMAGVLLI LLPIFTLMTL DRLERQKEFS FQRLLEKGVS LIRTFEAGTR
TGMFTMRWGA QRIQAMLLET SFQPEVVYMM ITSKDGRILA HSDAAMVGQI FDAMPDTAKI
NKDTAKVYHR VRQQKDKDEV FEVFKRFVPI RPRFKRGHMR MHGMPIRLQD NLPNRQESFQ
DRQERQRETM DWSRPYFQGQ GEELTEMAEH YLFAGLSMER EKFARTRLLK ETVWRGTFFF
LLGCAGMVAL FAFQAYRSAR ASLTSVKAFS DTVIQNMPSG LVTMNLYHDI TSVNRSAKKI
FGGDLTSPFP QLVELIELID EMTSSQEMVN REITLKSVSG SNIRLDVTAS PIRDSENQVM
GFLFLFRDLT QIWELKKQVE TNKRLAAIGK LAAGVAHEIR NPLSSIKGFA TYFSKRYEDN
ATDSETALIM VKEVERINRS ITQLLEFAKP MVVEKKQVDL HDLVDHSLKL VHHDLIQKKI
ETKVDIDLKQ PFIYTDGDRM NQVLLNLYIN AIQALGDRGR LEIRVQDAAK IPGHIEIRVM
DNGSGIDEQA IDLVFDPYFT TRSTGTGLGL SIVHRIIENL NGSIRVESTK GRGTCFIINL
PVS
//
