ID E1QDE9_DESB2 Unreviewed; 993 AA.
AC E1QDE9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Deba_0089 {ECO:0000313|EMBL:ADK83468.1};
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:ADK83468.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK83468.1, 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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; CP002085; ADK83468.1; -; Genomic_DNA.
DR RefSeq; WP_013256924.1; NC_014365.1.
DR AlphaFoldDB; E1QDE9; -.
DR STRING; 644282.Deba_0089; -.
DR KEGG; dbr:Deba_0089; -.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG4564; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000445_114_51_7; -.
DR OrthoDB; 5483045at2; -.
DR Proteomes; UP000009047; Chromosome.
DR GO; GO:0005886; C:plasma 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; 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; 4.
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; IPR033480; sCache_2.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF17200; sCache_2; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01049; Cache_2; 1.
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; 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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ADK83468.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW Transferase {ECO:0000313|EMBL:ADK83468.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..299
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 303..355
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 356..409
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 434..484
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 485..554
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 629..852
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 875..991
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 593..623
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 926
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 993 AA; 109900 MW; AD4ABEB9D122F933 CRC64;
MKRYLGAVLP ALLSVILFGV TVFGFLLPEV ESQIIAKKRE MIRELTNTVW NILATYDAQV
RGGLLDKDEA QRRALGRIRA LRYGPEGKDY FWVNGLNEVM IMHPYRMDLE GQRLPQFKDI
KGKDLLHAFV DVARQHGEGF VSYYWQWKDE PGQLKEKTSY IKLFQPWGWV VGTGLYKDDV
EAEMRAMNRD MSLVGAAVLL LVTLLSGYLT YREMRAEGER AAAQEVLRQT LDKYRAVLEA
SPDPVIVYNY VGLVDYVNPA FSRVFGWRAD EVLGGKIDFV PDDEKEATLA AINAVYDHPD
GLLSFESRRL TRDGRARNVM VSLAVYRGDG GAPLGMVVNL TDITSMKRSA EALRESEEKF
RSISANALDG VVMIDPQGRI TFWNQAATAI FGYAADETLG RELHPLLAPP RYHADYVKAF
AEFGDSGTGK AVGRMLELVA RRKNGQEFPA ELSVSSLQLH GQWYAVGIVR DITERKQAEE
ALRQSESRYR TILETVPYSI AISDLRSGAN LEINDGFCLL SGHSRQDALG KTALDLGLYN
RPEDHLTLRD QLERDGEING QPVTYRAKDG RLLECLVSVR RFVYAGRPCL LSVAQDVSAL
RQAEREQARL QAQLQRAQRM EAIGTLAGGV AHDFNNILQA ISGYTQLIGG HPGLDQKVRR
YAEDIDLAAR RATDLVKRLL TFSRKVEPAL QKVDLNRQID HAVAMLERTI PKMVRITTRL
DPDLKAVKAD PGQMEQVLMN LGTNARDAMP EGGELMIETQ NVRAEDLSPG AACQLTADEY
VMLRVSDSGM GMDAETQKKI FDPFFTTKGV GQGTGLGLSI VYGIIEGHGG RISCYSQPGQ
GTVFEICLPV ADDSLTEREA PEVVTVRQAQ SNGETILVVD DEAAILDVST ELLQGAGYKV
ITARCGEDAL EIYRTRGQAI SLVIMDLGMP GMGGQRALQE LKRLDPEVKV LISSGYSGDG
PVKDSLAAGA LGFIMKPYRL GDLLEKAHLA IQG
//
