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Database: UniProt
Entry: I4D0Y7_DESAJ
LinkDB: I4D0Y7_DESAJ
Original site: I4D0Y7_DESAJ 
ID   I4D0Y7_DESAJ            Unreviewed;       711 AA.
AC   I4D0Y7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Desaci_0394 {ECO:0000313|EMBL:AFM39461.1};
OS   Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM39461.1, ECO:0000313|Proteomes:UP000002892};
RN   [1] {ECO:0000313|EMBL:AFM39461.1, ECO:0000313|Proteomes:UP000002892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22704 / JCM 16185 / SJ4
RC   {ECO:0000313|Proteomes:UP000002892};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003639; AFM39461.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4D0Y7; -.
DR   STRING; 646529.Desaci_0394; -.
DR   KEGG; dai:Desaci_0394; -.
DR   eggNOG; COG2770; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_023166_0_0_9; -.
DR   OrthoDB; 9764522at2; -.
DR   Proteomes; UP000002892; Chromosome.
DR   GO; GO:0005886; C:plasma 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   CDD; cd18774; PDC2_HK_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; IPR033479; dCache_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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_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; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13188; PAS_8; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFM39461.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFM39461.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          311..364
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          493..708
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          349..376
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   711 AA;  79526 MW;  EDF6A76F705D3EEE CRC64;
     MNNSSIPWWM RIKVHFLLFG VTMSILPLFF LGYLGFTSVR QNLEKDIYAQ NFEQVTVLAH
     ELKDTFANLE NSLTLTKPTS AYALVGKDKT LRQVILETLL QKDPLIEKIQ VSDINYKVID
     QISYQEGVSA PSPAAKLENI ISPGTFPAIS KVLYTHDKRP KIYLTVTIQD PATKRNIGYL
     QAQIDVNRII NRYDSLQLGE GEYIFFVDQT GNLMGTSDSF LRLHPDKIRD NAAVQSFLDG
     KAYSQGSEYK SLSGISVVGS YTSVGSPNWA VVIEQPTREA NKPINEFALR LIIIAILIMV
     LVMILSIAFG LQVVHPIENL EAQVQQIIST GNLESHIPIE SWDEIGRLVK SFNQLLNSLD
     EKNENLKNEK ELLTTVVDGV GAGMVLLNTE RRIIWWNSKF AEWFGDNLAD SPCDQVVNVK
     ESENVQLENG RTISVFVHEE RRYFRQMYYN LSPDNPENAA YLLLLDDVTQ EVEMEARMIE
     TDKMAAVGLL ASGVAHEINN PLAIVAAHCE DLLDRMNEEE PQPTTEEFKG GFKIVLEQIV
     RCKKITDRLL GFARKRSNEG TDLIDIAAAS MQAVELIAHK AKQKQLEIKL QLESSLYSLG
     NENEWQQVVL NLLTNALDAS PESGIIEVKG YRDGETINFI VQDYGEGISQ ANLKKAFDPF
     FTTKSIGQGT GLGLYVSYGI VLKMQGAMAL ESTEGQGTCV KITLPFHKAG D
//
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