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Database: UniProt
Entry: I4CCX6_DESTA
LinkDB: I4CCX6_DESTA
Original site: I4CCX6_DESTA 
ID   I4CCX6_DESTA            Unreviewed;      1164 AA.
AC   I4CCX6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Desti_4800 {ECO:0000313|EMBL:AFM27417.1};
OS   Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC   Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC   Desulfomonilaceae; Desulfomonile.
OX   NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM27417.1, ECO:0000313|Proteomes:UP000006055};
RN   [1] {ECO:0000313|Proteomes:UP000006055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC   {ECO:0000313|Proteomes:UP000006055};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA   Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL   Submitted (JUN-2012) 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; CP003360; AFM27417.1; -; Genomic_DNA.
DR   RefSeq; WP_014812524.1; NC_018025.1.
DR   AlphaFoldDB; I4CCX6; -.
DR   STRING; 706587.Desti_4800; -.
DR   KEGG; dti:Desti_4800; -.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2204; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_51_7; -.
DR   OrthoDB; 9813024at2; -.
DR   Proteomes; UP000006055; Chromosome.
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; 3.
DR   CDD; cd00156; REC; 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; 3.30.450.20; PAS domain; 5.
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; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 2.
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; 6.
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); 5.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 4.
DR   PROSITE; PS50112; PAS; 4.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006055}.
FT   DOMAIN          153..223
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          227..278
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          279..349
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          354..405
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          406..478
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          481..533
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          534..576
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          731..787
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          800..1023
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1043..1159
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          122..156
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1094
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1164 AA;  131933 MW;  0F168358D02D144C CRC64;
     MPFEGDLGTA LQDEEPFTFR EWARILPVPT ILLNANFTVN TVNPACKSLG SQLAKLRGLP
     FSNLFPDPSE SSLVQNMLEH IISDGKIRTC KAHLRIADRE MRVDLTGRRF SQKKRNFVLL
     VIDSLASEKE HARKVVKKAI EEREKAERAL AESQTRFEQF VAHVSDIIVT TDIKGCFTFV
     NPPGLKLIGC TAEELLGTRF FDLVHPAYRK RAEKFYSTQF AKRKATTYYE VPVIDRSGKI
     MWLGQNVQLL FETDRIIGFK AISRNITDRR LAEDELKKSQ RRYKDLFENA NDVIYTHDLK
     GNYLSVNDAI TRILGYEREE FLKSRYQDFI APSSLPLVRE NLRLKVEQGI QCTGPYEILV
     RSKSGKPVWM EITSRLMLKE GKPIGIHGIA RDVTDRRLVQ DRLNESQELY SIVTEQTGQL
     IYEYDPATGK VKWSGAIEAT TGYTIQELVS DTRGWRKLIH PEDRFEAVAA FERAVARGVS
     FQIDYRFKRK DGTYIWIEDK GLCQKDESGS VFRVLGIMKD ISGRKHVETA LDLERKKFQI
     LVDNAPFALM MLSQSNDLAY VNPKFKELFG YDLQEVPNGR EWLRKAFPES AYRKQVIASW
     MQDMRKGATG EQRPRTFKVR CKDGTDKLIH FIPVQLSTGD QIVSCEDITY RIQGEKALQE
     RERFLASVFS CIQDGLSIMD KDLRIIRTNA TMQKWYKHDE PLIGKKCHEA YQGIDEVCPS
     CPALQTLKTG QATSFVIPKG GPANSITGWL DVCTFPLVVE SSGEIEGVIV HLRDVTERRH
     LEEQLRQASK MEAIGTLAGG LAHDFNNLLQ IVLGYADLLL LGKNKAESDY QRILAIRTAA
     KRGSDVVQRI LTFSRKVETK LRPVNLNQEL RFMEDLLRST MPKNIAVKLQ LAENPVMIQA
     DPTQIEQIVL NLAVNAKQAM PKGGNFVLET RTVDLDRDYC RTRPETKPGK YVMLMVSDTG
     KGMDKDVLDR VFEPFFTTKQ PGEGTGLGLS IVFGIVKSHL GHITCSSEPE VGTVFKLYFP
     LLKEQFESFA ETTQQMPAFG SETLLMIDDE ESIRNLGKEL LNEAGYNVLT AGSGQEALRI
     YREIWEGVSL VILDLVMPDM SGLECLEELL KVNPDVKVLI ASGYSPANQG REILELGAVG
     FVSKPYNFKQ ILAAVRAALD YRHK
//
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