ID M1PDP1_DESSD Unreviewed; 581 AA.
AC M1PDP1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=UWK_01277 {ECO:0000313|EMBL:AGF77840.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF77840.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
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; CP003985; AGF77840.1; -; Genomic_DNA.
DR RefSeq; WP_015403532.1; NC_020304.1.
DR AlphaFoldDB; M1PDP1; -.
DR STRING; 1167006.UWK_01277; -.
DR KEGG; dsf:UWK_01277; -.
DR PATRIC; fig|1167006.5.peg.1408; -.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_89_29_7; -.
DR OrthoDB; 9773941at2; -.
DR Proteomes; UP000011721; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011721};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 210..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 307..361
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 374..580
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 149..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 64866 MW; CE59B613500B829B CRC64;
MMPSTHQPFK FSKPALVLIL ASCLLAVILA FTTVRNLNRE QRLLENSLLQ QGLTLIRSFE
AGARTSMMHY MSGSNPLETL VEETTKEESV VYIRILHENG ESVAEAGDLP PPIDKEEVQR
ILDAESPVTR TIPEKSVFEL ARIFEPLPPL MPRRGRKPTP SSPSNSMRGK MYQHMQMMQE
EMQNKGRQLI VVGLGTSAFD TARQEDKTRA LLMGALLFLL GSAGLYFLFL YQSIRVGKST
LVNMQLYTDN VIESMPAGLI TLNSSNAIVS CNKKAEQLLS RRFSEMNNLQ PQELFSSFTD
DQQQDQLLIE SDVLCHNPLG EDIPVKLSTS PLLDHNGKKT GLVIILRDMR DIRKVEQQLE
LSRRLASLGK MAAGVAHEIR NPLGTLRGFA QYFGTRSEPG SDGKKYADLM VSEVDRLNQT
ISSLLQFARA REPQRIQVKA EELFGKLSSL MEVDFAAHQI DFQKDYDSEL VFNADPDLLL
QVLLNLLKNS ISVTENGGTI LLAAHKKNDD ICIEVSDTGH GMTDEEQEKL FDPFFSTRKD
GTGLGLAVSH QIIEQHHGRI EVESTLGKGT TMKIILPGEQ V
//
