ID I3Y6V9_THIV6 Unreviewed; 2046 AA.
AC I3Y6V9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Thivi_0673 {ECO:0000313|EMBL:AFL72727.1};
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:AFL72727.1, ECO:0000313|Proteomes:UP000006062};
RN [1] {ECO:0000313|EMBL:AFL72727.1, 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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003154; AFL72727.1; -; Genomic_DNA.
DR STRING; 765911.Thivi_0673; -.
DR KEGG; tvi:Thivi_0673; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2984; Bacteria.
DR eggNOG; COG3290; Bacteria.
DR HOGENOM; CLU_233185_0_0_6; -.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000006062; Chromosome.
DR GO; GO:0016020; C: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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 4.
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; 4.
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; 4.
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; 2.
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; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 4.
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; 2.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 370..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 405..453
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 540..613
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 618..670
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 853..923
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 996..1053
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1304..1527
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1544..1666
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1703..1819
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1866..1968
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1598
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1752
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1905
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 2046 AA; 224641 MW; DB1FC7E862C5727F CRC64;
MNLVVTWRYE ALTAPPWRSG EKLAHSGRGW RRLLLALLML ALALPVPFAR AVPKHPSEVV
ILNAYHPGDD WSDSELAGLL EAFRQVRPER PPAIEYLDTK RFPGSDYPSL LKEFLVRKYR
DRPVDLVIAL DNPALDLLSA FPHELFAGVP VVFGGISGVP PERLRERGNI TGVTEVLDLA
GSLELLLRLH PRTQGILLVN DDTATGRAVR RKMESVLPAF RSRARIEFAP AGTFAELTRQ
VAELPPDWVV LMLSYVTDQA GQVFSREDST RRISAASPAP LYAMHAVRLG HGIVGGLLLD
GRQHGAQVAV LALRVLAGED PGQIPVEQSR GLPAFDAERL QHFGLRIENL PPGSLVINRP
LSFYSLNREL VWGALAAFLL LSLVVLVLGR ALLHAQRAEA ARRASESRYR NLFETMAQGV
VYQDADGHIL SANPAAQRIL GLTLDQMQGR TSLDPQWRAV REDGSDFPGT DHPGMVALRT
GHEVSGVLMG VFNPEREDYR WINVHATPQF EPGAPRPYQV YATFEDVTEQ KTAADALRES
EERLRLATRA TNDVIWDWDI PRDAQRWNEA GTLVFGWTEP VEHPVSADWW LERIHPDDRP
RVAARFHAAV ENADCDRWQD EYRLRRQDGN DALVLDRGYI MRDAQGHALR MIGAMLDLTE
RKRAEERLAR LARLYQTLSD TNQAIVRIVD EGELFERICA LVQQLAGFRL VWIGLHDPAR
NRLIPRAARG ENAEILLRFE LSLDPETPEG QTLAADCFRD GTVILCNDCQ AFGEHERGRR
LPFKEGLSAI VCLPLFRNDQ TVGVLEIGST ETGYFDDEVM GLLREMASDI SYALDNLERA
RILDETLGRI ERQRSFYEGI LEKVHDGIFV TDAGHRILYA NAALCEISGL PVEAIRGRQV
LEEFPEETLR EFRPLYLNVM ESRQSLPYEI QVTTPAGREG WQAGWLIPTS ERDAFAGMIC
TVRDISETHT AQLALEQYKI GLEKTVERRA AELRESEEFL RLILESSAGG LYGLDLEGRI
TFVNPAACDL LGYPTDRLLG RNSHALFHNR RPDGSPYPPE NCPACATLRE GRSATVDDEV
FWNADDRPIP VSYSIRPMLR NGDIVGAVVS FLDLAERKRL EEKLRRLAGA VEGIAGVRDL
ASLAAIVCAA ARQLTGADGT TLALRDGDDC ACLDEDAIGP LWKGQRLPLA ACVSGWTIQQ
AEPIVIEDRA HDPGILSGTP EDVDSRTFVR GLSLVPVGRS DPAGALGCYW ARPYRISVEE
LGLQQALADA TAVGLNNLDL YRRLEDARAL AEHLTQIKSV FLANMSHEIR TPMNAIVGLA
HLLQREIRDP EQRDKLGKLM TAADHLLTII NDILDFSKIE AGKLSLERID FELDEVLDRV
CSLVSGQARA KGLELVLDLD ERLSGAPVLH GDPTRLIQML LNYLGNAVKF TEGGTVTLRG
WVEAEEGDDW RLRFEVRDSG IGIAEEHRSR LFEAFGQADN STTRRYGGTG LGLAINRRLA
QMMGGTVGVE SQPGAGSTFW FTARFGKAHP SGRRPEVMRL RGRPVLLVEH QPETRTALRE
MLVHLGLRVT AVDDSPAALA AVAEADTAQD PFVLALLDGD MPDSDGLETA RRLRALPLIQ
PPTLLLVDRH ADDAARCAAA RAAGVRVCLA KPVTPSALHD ALIRALDASI VGPRGLRLAA
DTGSSMQPSA VERELAAAHR RARLLLAEDN RINQEVALEL LRAVGLQVDL ADDGARAVEM
ARAIDYDLIL MDVQMPAMDG LEATRAIRRL PGRSDTPILA MTANAFAEDR EQCLAAGMND
HVGKPVEPDA LFAALLKWLP PAGSGALPAT PPEPVAVAAS PAPALADLAA IPGLETASGL
RGVRGKADVY RRLLTTFADH HGGDMAALRA CLANGDRETA RRLAHTLKGV SGTLGATGVQ
ALAASLETAL RDAGSSTDLE PTIASLDTEL VALLDGIRCH LAPPAPPAES SPDRDRLRAV
LSELMGLLAE NNTRAAQVAH AHADLLHRAF GPAAVDLERR IDDFDYETAL QTLDALLTAS
PDWLEV
//
