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Database: UniProt
Entry: M1PS13_DESSD
LinkDB: M1PS13_DESSD
Original site: M1PS13_DESSD 
ID   M1PS13_DESSD            Unreviewed;       490 AA.
AC   M1PS13;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=UWK_02615 {ECO:0000313|EMBL:AGF79151.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF79151.1, 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; AGF79151.1; -; Genomic_DNA.
DR   RefSeq; WP_015404837.1; NC_020304.1.
DR   AlphaFoldDB; M1PS13; -.
DR   STRING; 1167006.UWK_02615; -.
DR   KEGG; dsf:UWK_02615; -.
DR   PATRIC; fig|1167006.5.peg.2832; -.
DR   eggNOG; COG4191; Bacteria.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_000445_89_29_7; -.
DR   OrthoDB; 224978at2; -.
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; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
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   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGF79151.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          190..242
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          259..471
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   490 AA;  54484 MW;  5333D036996B2511 CRC64;
     MFALNLRQKM IGCFCLHLLF YIIVGITFLK DFNMFNDDVT LLMHAGNLSN ISLEIRRYEK
     NFIIRHDNTD FNKVLEYVDE AQQFVPQVID DLQIMPHPTH LQDLTAKLTA YEETFKEFKG
     KCTIGQDVTV CPLREKVRSL GQELVNITED LVLFEQNKMT VFIEKFTIRL INTVLFLVLL
     SVFTISLLYT SIVKPLKKVE NAAIDIANGT FSRLSVDDKK GEVRSVLRAF NKMVTDLEEQ
     QEQLFQAKKL SSIGTLASGT AHQINNPLNN ISTSCQLALA NMGDDKDSFV ARMLKTIDQE
     TQRAGEIVRG LLEFSRAHTF SSQPCQLAKI VNKVKLLVAS EIPTGINIET DIPEDVVLYV
     DVQKMVEALL NLTINAIQAI PEPPGTVCIK AEKDEEQKKA VITVADTGTG IDPENLAKVF
     DPFFTTKTAG NGTGLGLAVV YGIIKKQGGS IRVESTKGTG TNFIITLPLH SEPAETMLPG
     KYSTSRGTNV
//
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