ID K0NQ64_DESTT Unreviewed; 1267 AA.
AC K0NQ64;
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 OrderedLocusNames=TOL2_C41470 {ECO:0000313|EMBL:CCK82303.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK82303.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK82303.1, 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; CCK82303.1; -; Genomic_DNA.
DR AlphaFoldDB; K0NQ64; -.
DR STRING; 651182.TOL2_C41470; -.
DR KEGG; dto:TOL2_C41470; -.
DR PATRIC; fig|651182.5.peg.4878; -.
DR HOGENOM; CLU_000445_89_20_7; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0016020; C:membrane; 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; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; 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; IPR013767; PAS_fold.
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; 4.
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 Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCK82303.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:CCK82303.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1267
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003835305"
FT TRANSMEM 338..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 372..425
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 446..497
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 498..564
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 569..621
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 622..694
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 698..751
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 828..880
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 900..1124
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1143..1259
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1194
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1267 AA; 144144 MW; 769E164173FD5B80 CRC64;
MWIPLCFFFV LLFTSFSNSS EAKKKNILIV FSYEYGMPAY NIVEQTIRSE LNTDNSNIIY
FNEQLDLSRF IGEKYKNTLK ESFYLKYNHL KFDLIITIMK PAFDFIQSEC KDLFPGVPIV
YGLIDEGFDK PKKLPANTSG FAMNVSIDGT IKAAMKIQPD AQHMVIVSDK TQLGQLLEER
AKQAIDTIPD QISVTSLSNF SMEKILIKVH NLSSDTIVLY LVMSEDGDGK PIISTDALKM
ISDVSNAPVY GLWDILLEHR MTGGCLSSFV SLGRNMAEKG KQILNGQIES PSLITIPNTH
MFNWRQLQRW GIKEQNLPSG SRIKFKEMSV WDTYKKQILI VFLICISEAI LIGFLLVQRR
KTKLSEIKRS KTKKFRDNLI KTANVLILGF DTQGNVTLLN SAVEKLTGYL TSEFEGKNLF
NILVPGKSDQ AAGHLFNNFM NESLPKLSEY KIQTKDGRER IILWSNNAIK QNGKVEGTIL
IGIDITERKH AERLLKESEE KYRELIDNTS DISYRSSIDG YLIFLSKAVQ RLTGYTVEEA
IGSNIADMYL YPEERKKVMA ILKKWGHISD YEVQFKHKDG SIWWASSNSQ LFTDQNGNIL
GVEGTIRDIT RRKIAEEELR KNEERLRLAL EGTNTGFYEW YPVTNETYFS PTFFTMLGYE
PDKFPHNYNT WADLLHPEDK LAAETVVKDF LQKRQSSFKH EFRIRSKKNG YHWILSRGAA
MEWDEKGRIQ RIIGTHSDIT DSKLAEEMLR DREMRLRTMF DQTFQFMGLL SLKGNLLTVN
RVALEFIKAK EADVIDKLFW ETPWWTHSAK EQKKILQAIK KAALGEYISF ETTHIDPSGN
LHHIDTSLKP ILGDDGRIIY LCAEGRDITD KKQGQKERVK LEKQLHQAQK MEAIGTLAGG
IAHDFNNILG AIIGFSELAL EDIKEGDPVR YSIDQVLQSA FRAKELVEQI LLFSRQGKHK
MKPVKITSLI KEVIKLLRST LQKTIDVKEN ILIKKDMVLA DPVKIHQILM NLCTNSAHAM
GEKGGTLTVT LDQIDFDKKS LMEFSDLKSG SYLKLKVTDT GHGIPEKLID KIFDPFFTTK
PRGEGTGLGL AVVHGIVKDH KGNIKVYSEP GKGTAIHIFL PLLKADDPLA VKDDKPISGG
TEHILLVDDE IPLIKFGKQT LQRLGYRVTA FSDSRIAWET FQKNPNFFDM VITDKTMPEI
TGLMLSEKIV NLCPEIPIIL CTGFGDELSL KEAEKIGVKA MLHKPVIKKD LAETIRRVLD
QTREKGV
//
