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Database: UniProt
Entry: I3Y8C0_THIV6
LinkDB: I3Y8C0_THIV6
Original site: I3Y8C0_THIV6 
ID   I3Y8C0_THIV6            Unreviewed;      1347 AA.
AC   I3Y8C0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Thivi_1215 {ECO:0000313|EMBL:AFL73238.1};
OS   Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS   violascens).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocystis.
OX   NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL73238.1, ECO:0000313|Proteomes:UP000006062};
RN   [1] {ECO:0000313|EMBL:AFL73238.1, ECO:0000313|Proteomes:UP000006062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17096 / DSM 198 / 6111
RC   {ECO:0000313|Proteomes:UP000006062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA   Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of Thiocystis violascens DSM 198.";
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; CP003154; AFL73238.1; -; Genomic_DNA.
DR   STRING; 765911.Thivi_1215; -.
DR   KEGG; tvi:Thivi_1215; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3706; Bacteria.
DR   HOGENOM; CLU_005763_0_0_6; -.
DR   OMA; WTQDWEY; -.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000006062; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT 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; IPR036641; HPT_dom_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; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
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:UP000006062};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          288..340
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          589..640
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          672..893
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          912..1033
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1070..1190
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1244..1341
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   REGION          632..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          39..66
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         966
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1120
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1283
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1347 AA;  148324 MW;  BCEEE8D7A490A845 CRC64;
     MISSPKKLLT DASSDHDQIR ARAKQALDSG DFECVDKYLS ETEIDLAELV QNLRIYQVEL
     ELQNAELRVT QTAAERMAAR YNTLFSSIPQ AVLVVDRHGM ILEANHAACR LFDLRQGHRR
     NHYLPRLVAR ESETQLDDAL KLAHESSASR SSDMRFLTTN GGSFEGELQV ARLPLDEDGE
     CQFICSVVDL SERLRQKAII SAAYARSRES EARYRILADY SADWDYWLGP DGRYRYVSPA
     CESICGHAPD IFLADPDVMR RLVHPDDHPL WMAHASEATP ACCATPLVKL ELRLCRPDGE
     MRWIEHQCRP VYDGEGTRLG WRGVNRDITQ RKQAEIILDL QKRRADALLE LPHAAEGRGD
     AAFMQHSLGL AESLTGSAMG FMHFILDDQE TIEFVAWSRA TLEAGCPIAT GNLHAPIGEA
     GLWANAVRQG QPVVCNDYAA ATDKKTLPDG HLNLQRFISI PVMDAGLTRM IAGVGNKPTN
     YTALDVESVQ LIANATWRIV HQRRAEQALI KSEGRFRNLS SLMSDIAYSC VEVSPNRFTL
     DWVHGAVASI TGHTAEAIIA MGTWRRLVIL EDRPLFDRHV SGMVTGEATT CQLRLRRRHG
     GLTWVEITNQ CVLDPDGCRR VYGGVKDISE RKQAEQQLEQ SAQQMERQNR ELDRALAEAE
     ASTQDKSRFL ANMSHEIRTP MNGVIGMTRL LLETGLNEEQ HRFAEIARTS GESLLALIND
     ILDFSKIEAG KLELDLLSFD PRGTLEDVVE LLAFNAQSKE LELTYQIDPD VPVSVRGDPR
     YLRQILVNLA GNAIKFTDHG EVAIHVKAAT KTADKVLIRF EIHDSGIGIP EDLRGHLFTA
     FSQLDNSSTR RFGGTGLGLV ISKQLVELMN GAIGVESRAE RGSIFWFTAE FELPAVQPVA
     PLPTYADLKG GKVLVVDDHA TNRLLAGTLL RSWGCRIEEA NNGAEALEWL HQAARAADPF
     QAALLDLKMP AMDGLELGNL IKQDPEIRDT RLVLLTSLVA RGDAARMQQA GFDGYLTKPL
     RQQLLHDCLA LVMGREVATL RAAPPAIVTR HTLADINRQA LGASASSQAR ILIVDDNLTN
     QIVATGILKQ LGYSRTATAS NGLEALEALA RDPYELVLMD GQMPDMDGFE TARRIRLGEA
     GTANRDVPIV AMTALVMQGD RERCLEAGMD DYLSKPVQPL ELAAAIAAQL APASAPPSAL
     RAASREPATP RIDRTTAAPT SDQRPPPSQA VFDEADMLYR VMGDRQIAAV VIEQFLSDAP
     TRVLELKACL GAGDLAEAHF KAHSLGGLAA NISAPRLREV ASSLEMLEMT ADNAGALAQA
     LQLAQRVEDE FSQLRTVLGE WLNQTSA
//
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