ID C7LQS5_DESBD Unreviewed; 1121 AA.
AC C7LQS5;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Dbac_1041 {ECO:0000313|EMBL:ACU89154.1};
OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378 / X)
OS (Desulfovibrio baculatus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfomicrobiaceae; Desulfomicrobium.
OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU89154.1, ECO:0000313|Proteomes:UP000002216};
RN [1] {ECO:0000313|EMBL:ACU89154.1, ECO:0000313|Proteomes:UP000002216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4028 / VKM B-1378 / X {ECO:0000313|Proteomes:UP000002216};
RX PubMed=21304634; DOI=10.4056/sigs.13134;
RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., Del Rio T.G.,
RA Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Meincke L.,
RA Sims D., Brettin T., Detter J.C., Han C., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Desulfomicrobium baculatum type strain (X).";
RL Stand. Genomic Sci. 1:29-37(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; CP001629; ACU89154.1; -; Genomic_DNA.
DR AlphaFoldDB; C7LQS5; -.
DR STRING; 525897.Dbac_1041; -.
DR KEGG; dba:Dbac_1041; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2984; Bacteria.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_89_20_7; -.
DR OrthoDB; 9813024at2; -.
DR Proteomes; UP000002216; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
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; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
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; 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; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACU89154.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002216};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ACU89154.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1121
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002979372"
FT TRANSMEM 340..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 374..412
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 440..492
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 493..536
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 567..619
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 694..748
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 761..983
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1002..1117
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1053
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1121 AA; 125897 MW; FA7D87203CDCB66C CRC64;
MRNIFFCLLM FLFIPHAFGQ DEKKINVLYI NSYHNGYEWS DSIFDGVREK FRSSGKNIYL
QIEYMDSKRY SGEKINEILF NYYKFKFKTT HFDLIVTSDN NAYEFISEHG EDLFPNVPIV
FCGINDVEAG QVPMRSRMTG VLEEFEVPWN IELALQFHPG KKRLVVIGDQ SMTGVAIANQ
VRAQVPGLPK EIEVEFLDEF TLDELVAKVR FASADSIFFF IPFYKDVGEA VYSAQDLLEI
VWRETGVPLY SAWEFLLGHG MVGGKMISGF SHGQAVAEMG LRILDGESPA DIEISISPDD
PPKFDYRVLM RLGINQNLLP EGSILINEPS PFYSINRHQF WTIIISLVIL SLVLILLVIN
IWERKQIEVR IKNQLSFLRT LMDTLPIPIY FTDRSGAIAG INRAFEHWFG VSWEHDKGFE
SQELALVETR FAPLLDLRMD SYEAQIRHGD GTLRPAVLHK ATYADAQGEN AGIVGVIYDI
SDRKKAEDDL RAAEEKYRTI FENSALGIFQ TTPDGSWMVA NPALARMLGY ASPEALIAGN
PNISSLYFQQ SDRERVVDLY QQNRGSVEFE VLFRTRAGEI ITANLNARAV RGCNDDFCHF
EGFVEDITDR KAAELALAAS EAMLQLVLDT IPQLVHWKDR ELRIIGANRN FLAHVGQTEL
SVIYGKKYAE VVSYAHEVEQ ISRLDQEVVE TDEPRFRLRL ETRNLAGENM WLLVNKVPLH
GPHGEVVGIL STAEDITQTM NLEKQLLQSQ KMEAIGTLAG GIAHDFNNIL TSIMNSTELA
MEDIPEDSLN WKDLERSLKA AVRGSGLIKQ ILTFSRPTQE GFLPTDLREV VSEAVALIRV
SMPRNITVLA EIEDDLPLCL ADPTQVHQIV MNLATNAFQA LGEGGGNISI RLSKMILDRD
DAQLGNLVPG VYSRLCIEDD GPGIDEDIQD KIYDPFFTTK GKGEGTGLGL AVVHGIVRNH
GGEIRLVSTA GFTRFDILLP TMNELCLLPG ECAGALAMGN ERLAFIEDDE DQLLLIPRVL
EQLGYEVHSF QNPAEAVFTL CEEGLPFDLV ITDFDMPGMN GFDVAGILQE RRPDLPVIMV
SGRKQAEEFL GQAGNIKFFL SKPYNKDMLG RAIRDVLDKE A
//
