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
//