ID E1QDZ2_DESB2 Unreviewed; 1157 AA.
AC E1QDZ2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Deba_0403 {ECO:0000313|EMBL:ADK83778.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83778.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK83778.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
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; CP002085; ADK83778.1; -; Genomic_DNA.
DR RefSeq; WP_013257234.1; NC_014365.1.
DR AlphaFoldDB; E1QDZ2; -.
DR STRING; 644282.Deba_0403; -.
DR KEGG; dbr:Deba_0403; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_7; -.
DR OrthoDB; 9806821at2; -.
DR Proteomes; UP000009047; Chromosome.
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 CDD; cd17534; REC_DC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 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; 3.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
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; 5.
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; 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; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADK83778.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW Transferase {ECO:0000313|EMBL:ADK83778.1}.
FT DOMAIN 8..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 135..206
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 209..262
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 513..568
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 637..706
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 709..761
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 781..1007
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1026..1142
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 445..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1077
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1157 AA; 125567 MW; 8523ABC04EDEB607 CRC64;
MTPPAKASLL IVEDEFIVAQ HLRASLESMG YEVAGLADSA AEAVELAERL RPDLVLMDIF
LAGPSDGIEA AMTIRRRLGR PVVFLTAQLD DDIIPRAAAA QPHGYLNKPF KIKEVQAVVE
TALHKAAMEA ELAAGQERLR LILDATSDGA WDCDLRADRV FLSEKGLALL GRDGQDPHDL
AAWLGLVHPD DLPSLEAVAQ ALRQDAPTLD VQLRLLGADG QWRFLHCRGR AVAWRADGAA
GRVVGTLTDI TAQKADQAEL AEARERFMHL ARFTSDALLL IHDGKIVHFN PAHGQSLGYG
AADLEGVEFT RLLAPHDRRR VGGYHRRRLA GESAPEEFVA DIVDVDGQIK PMSLRSQLAR
HQGRQLVLTA MRPLKGHDAE TADSNGLTGA VLDNLPVGLA VFALDSGLCI YMNDNYGRVV
GWPKAELPSV SKILGRLFPD REERRKRLAD VRPGPASDGR QKRQWNNIAV QTRDHGRRYI
STMSIAVPDH GVIISTVWDV DSQRRAERAL AASEEKYRQL VENAGEAIVI VQDGAVRLAN
PSAARFFGLP PAELAGQNIA GLIHPDDRAK ALALYAQHQS AAAPPAAGPH RMLRRDLGPG
WVESRVAPVE WEGRPAVLAC LTDVTEAVQA QESLKERNET LQAMINASPL AVIGLNHRGE
VVLWSGAAQA MFGWDAEEVL GRFNPLAAPQ ERAEFERHLA RARDGRQALH LEMTCKAKDG
RPVDMTVHVA PVRGSDGRAG SLLCLVEDVS ERRRQERVWA RLEEHLSQNR RLEAVGVLAS
GVAHEFNNIL AAIIGYGELA KEDLQEGRID SPLHFLDNQM KAAERGRELV RQILAFSRHG
SGRRRRVDLA PVLAQQVRLL RAVVPANVAL RAELCEGPLS AEADPAQIQQ VLLNLTTNAV
EAFDGGDGSI IFQTDVAAFD EADAAAPPGL APGRYLRLRV DDDGPGMPQG VLERACEPFY
TTKKQNRNAG LGLAEAHGVI SAHGGRLILH SRLERGSRVE AFIPLCDKPL PAATEPGPAP
DQGCARILFV DDERSLVEIA QRLLTNMGHR VEAFGDARLA LQAFVDDPQA YDLLISDQSM
PHLSGLELAA RVTALRPGLP VIICTGHGQQ LTPQSLARAG VGQLLYKPVD KRELAAAIGR
AMAGRAAPLS TTGPLPS
//