ID C8W0J5_DESAS Unreviewed; 674 AA.
AC C8W0J5;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, 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=Dtox_2441 {ECO:0000313|EMBL:ACV63250.1};
OS Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV63250.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV63250.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
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; CP001720; ACV63250.1; -; Genomic_DNA.
DR RefSeq; WP_015757951.1; NC_013216.1.
DR AlphaFoldDB; C8W0J5; -.
DR STRING; 485916.Dtox_2441; -.
DR KEGG; dae:Dtox_2441; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_012281_1_0_9; -.
DR OrthoDB; 9816482at2; -.
DR Proteomes; UP000002217; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00075; HATPase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF13589; HATPase_c_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACV63250.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW Transferase {ECO:0000313|EMBL:ACV63250.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 518..674
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 674 AA; 77419 MW; 68413AE500CE7585 CRC64;
MPSFSFSASS KVKDLVGRRL VTNKHSALFE LVKNSYDADA DKVNVSFNIL EDTLTIDDDG
DGMSLNEIEN KWMVIGTDSK QGKLFTSKGR VLNGEKGIGR FSADRLGNKL EMIACVEESE
KAIRMIFDWN LFENTNYLLD DIQIDYSYID KPKLKGLTLI ISGLRDAWTI DDIVRVEKKL
SGLLSPVGNT DDFAIYLNCQ EYGVKNKQLI PYSISDISSI WINVEVPVND TDIINYRIYR
NGAELDKGSY NNTYNFGPVN VLIYSFTTGD KISFKHKFSI DVVNFGNIRI YRDNFQIYPY
GEHLNDWLGL DRRKTQGHFR NLGSREVIGY IQIYREHNKG LIDATNRQGL EENKDYDELK
QFIKKEALTK LESEFYFKKN KDIKSEARSN REEIIKTTKE VKEIAKKLFS VAPSEANELV
DLSNQLHDKT IEQDKIIRNQ LQVIEIYKRA ASKETLLQKI IHQAFIRAQN ISTAISNTED
DLKTIDINPD ARYIINKCHN FIKERASEIG DFLVSVREKI LKKREKININ IIKSIKRVIN
HYMPEFRENG IECIVEGDES LIIYFDPSDF KVILENLISN SKKALNKCNT NDKFIHIRVI
NNDSRINIFF RDNGIGIPPR DAAHVFIPFY TTTDGFGMGL AIVDELIKDN GGEIQLVQLK
PDESGAEFQI TFKR
//
