ID M1P584_DESSD Unreviewed; 714 AA.
AC M1P584;
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_02110 {ECO:0000313|EMBL:AGF78653.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF78653.1, 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; AGF78653.1; -; Genomic_DNA.
DR RefSeq; WP_015404343.1; NC_020304.1.
DR AlphaFoldDB; M1P584; -.
DR STRING; 1167006.UWK_02110; -.
DR KEGG; dsf:UWK_02110; -.
DR PATRIC; fig|1167006.5.peg.2296; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_104_15_7; -.
DR OrthoDB; 9758705at2; -.
DR Proteomes; UP000011721; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AGF78653.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000011721};
KW Transferase {ECO:0000313|EMBL:AGF78653.1}.
FT DOMAIN 203..424
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 442..563
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 593..710
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 496
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 644
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 714 AA; 79766 MW; 2D5D1AE2D0277635 CRC64;
MTDNFSIFDT VSSYEKEINE LLHLLFISVP NCFAICIDNK GQTHSKKSGS APDTSISEKL
QKLLQENREE YAVVSTEDNN WSAIALPEIK ATLYFTCPTH TDDTCIDNIQ FCCRLFGGHQ
KTVAAQKKLE IQKKQFDRKF SVLEAKYQAT LEDNEKSYRI IQEQQENYSK TLQTEIELQT
KELRKAKVAA ESASVAKSEF LASMSHEIRT PMNGVIGFTE MLLQTELDEE QRDSAETIKR
SGEALLGLIN DILDFSKVEA GQMSLEYIDF DPEITAHDVC ELVRPRVSGK PIEVLCKIDD
NLPANVCGDP GRFRQVLLNL LGNSAKFTEK GELELTINVE EEDDKNIKLH ALIRDTGIGI
DSSKCESIFE AFKQEDGTTT RKYGGTGLGL SICRKIASLM DGRVWVESTK GKGSTFHFTA
MMRKSSISRA KTLKQLDLEG TRMLIVDDNA ANNEILVHLL NNAGIKTTAL LDETQTMATL
KEAEECGAPF DLAIIDLQMP TITGFELARI IRESNLKSRD IPFLAYTSST EKIAKKCKDA
GFTAFLNKPA RRAILLRTLS RTLGTGGDEI DPAAEKKLVT QYSVREEIKQ SIRILLVEDN
LVNQKLASMI LTKAGYNVEV AANGKIAVDM FSSTPDLFDT ILMDVQMPEM DGYEATRQIR
KLGYTSIPIL AMTANAMKGD RELCLEAGMN DYITKPIKRD IVFNMLDKWL NSPS
//
