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Database: UniProt
Entry: M1PUG3_DESSD
LinkDB: M1PUG3_DESSD
Original site: M1PUG3_DESSD 
ID   M1PUG3_DESSD            Unreviewed;       864 AA.
AC   M1PUG3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=UWK_03444 {ECO:0000313|EMBL:AGF79961.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF79961.1, 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; AGF79961.1; -; Genomic_DNA.
DR   RefSeq; WP_015405643.1; NC_020304.1.
DR   AlphaFoldDB; M1PUG3; -.
DR   STRING; 1167006.UWK_03444; -.
DR   KEGG; dsf:UWK_03444; -.
DR   eggNOG; COG2197; Bacteria.
DR   eggNOG; COG3852; Bacteria.
DR   HOGENOM; CLU_000445_114_77_7; -.
DR   OrthoDB; 45683at2; -.
DR   Proteomes; UP000011721; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR029150; dCache_3.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF14827; dCache_3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:AGF79961.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000011721};
KW   Transferase {ECO:0000313|EMBL:AGF79961.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          496..722
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          743..858
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         792
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   864 AA;  97268 MW;  D98825BCE17249A0 CRC64;
     MTVNSNQDST KSSPSLSRPL LYRLMIPLST TILLLVLAFT TAFLMVHQQD MQRFNQHIMT
     DAGRSLKISL IRNAQMLNSM EDIFLKDRYL YEALQAQDRE RLRTLYGPIF EKLHEKYSIT
     HFYFHLPNRT NLLRLHKPNM HGDLIDRFTA RESARSGKTA SGIELGPLGT FTLRVVQPIY
     VAETLIGYIE LGQEIETLLQ AIHRRLGVEM AVTIHKDALD QKQWEAGMNM LGREANWNRY
     REEVLIYHSL PHFSSELDQF VHGNKDHRHN EITKKILFDN KSWQVLSHSL QDASGTDVGD
     LIVFRDITDS QEAFVQLAAI TAAMALILLS GLFTFFYVML RRSDNSIQAQ HAKLVESEGR
     HRSLLDAINR SGIFLFVVDG DYRVRYMNES MRETFGQASG KLCYHDVAGY ETPCSHCRLE
     EVIGSQKTVY YHSTLANGRT FNMIAVPYVD TDGTACKLEV MQDITRQRQV EDEKEMLEQK
     LQRAQKMEAI GLLAGGVAHD LNNILSGIVA YPELLLLKLP EDSELRKPIA AIQESGKRAA
     AVVDDLLTVA RGVARVKESC NLNLLIQEYL DSPEYKALRS LHPHVTYRHQ LEASHPVLTC
     SPVHIKKSLM NLVINATEAV TDEGSIIIST SNHYIDDAAA DAQNMRAGEY LILGVQDSGS
     GIPDKDLIHI FEPFYTKKVM GRSGTGLGLA VVWNTVEEHQ GKIFVESGEN GTLFQLYFPV
     SKKGEITQTM DAQAEILTGN GEHVLVVDDE PHLRDIASQM LHSLGYNVAS VCSGELAVQF
     VKEKPVDLLV IDMLMEPGMN GRQTYEAILK LYPDQKAIVV SGFSESDDVK TTLQLGANGF
     IKKPYTLEDL GRVVRRAFNC YNTD
//
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