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Database: UniProt
Entry: D3T123_NATMM
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ID   D3T123_NATMM            Unreviewed;       603 AA.
AC   D3T123;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Multi-sensor signal transduction histidine kinase {ECO:0000313|EMBL:ELY32710.1};
DE   SubName: Full=Receiver/sensor box histidine kinase {ECO:0000313|EMBL:ADD07282.1};
GN   OrderedLocusNames=Nmag_3740 {ECO:0000313|EMBL:ADD07282.1};
GN   ORFNames=C500_03399 {ECO:0000313|EMBL:ELY32710.1};
OS   Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS   IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS   magadii).
OG   Plasmid pNMAG01 {ECO:0000313|EMBL:ADD07282.1,
OG   ECO:0000313|Proteomes:UP000001879}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD07282.1, ECO:0000313|Proteomes:UP000001879};
RN   [1] {ECO:0000313|Proteomes:UP000001879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC   8861 / NBRC 102185 / NCIMB 2190 / MS3
RC   {ECO:0000313|Proteomes:UP000001879};
RC   PLASMID=pNMAG01 {ECO:0000313|Proteomes:UP000001879};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA   Maupin-Furlow J.A., Woyke T.;
RT   "Complete sequence of plasmid 1 of Natrialba magadii ATCC 43099.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADD07282.1, ECO:0000313|Proteomes:UP000001879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD07282.1}, and ATCC 43099 / DSM
RC   3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 /
RC   NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879};
RX   PubMed=22559199; DOI=10.1186/1471-2164-13-165;
RA   Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., Sastre D.E.,
RA   Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., Goodwin L.A.,
RA   Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J.A.;
RT   "A comparative genomics perspective on the genetic content of the
RT   alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.";
RL   BMC Genomics 13:165-165(2012).
RN   [3] {ECO:0000313|EMBL:ELY32710.1, ECO:0000313|Proteomes:UP000011543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC   8861 / NBRC 102185 / NCIMB 2190 / MS3
RC   {ECO:0000313|Proteomes:UP000011543}, and MS-3
RC   {ECO:0000313|EMBL:ELY32710.1};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [4] {ECO:0000313|EMBL:ADD07282.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD07282.1};
RC   PLASMID=pNMAG01 {ECO:0000313|EMBL:ADD07282.1};
RA   Pfeiffer F.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001933; ADD07282.1; -; Genomic_DNA.
DR   EMBL; AOHS01000012; ELY32710.1; -; Genomic_DNA.
DR   RefSeq; WP_004214207.1; NZ_AOHS01000012.1.
DR   AlphaFoldDB; D3T123; -.
DR   GeneID; 8826610; -.
DR   KEGG; nmg:Nmag_3740; -.
DR   PATRIC; fig|547559.17.peg.648; -.
DR   HOGENOM; CLU_000445_114_58_2; -.
DR   OrthoDB; 327291at2157; -.
DR   Proteomes; UP000001879; Plasmid pNMAG01.
DR   Proteomes; UP000011543; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd17535; REC_NarL-like; 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; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF08448; PAS_4; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 2.
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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ADD07282.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Plasmid {ECO:0000313|EMBL:ADD07282.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001879};
KW   Transferase {ECO:0000313|EMBL:ADD07282.1}.
FT   DOMAIN          16..131
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          152..215
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          262..303
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          336..387
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          391..600
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   MOD_RES         66
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   603 AA;  67229 MW;  1B35CA87C6AA0940 CRC64;
     MTSIPSELRD LAKTATVLQV GSDWSLADYP EFHTIEDVFL TLEHESDPER ALERLETTAI
     DCVVTDHELP KMDGLDLLTA IRSQYPALPI VLFPENGSEE LASEAIASGV TGYVPRTSPD
     AGQQLVEQIA QATASYEHHQ LTHQLDQNSA GVLEQLSDGI IVLDTEWTIT YANEGAQKFF
     QRPPADLIGH TLQELTPAIS TTSFYDHYHD VLDTGGSRRI EEYYEPQDRW YAEYIYPTDN
     GLTVVFRDIT AQKERERELE ETTAQLHALL DNVEAAVWIR DPDSRFVLLN QEYRTRYGIS
     REQPVVGHPP ETVVSDAIAA EIRARDQDVL ERESSLTFEE KRLTTAGYQT YLTRITPLFD
     ETGTVSATCG VSSEITTQKQ TKQHLDVLNR ILRHNLRNDM QIVHGYATEL VTELDGPTQK
     LAEQIQDQST ELIDLANDAG MVNQLLSQPL DLQSLSLPAV LSTVVSNLRS EYPDAIITVD
     VPSTAIVAAD RRLLTLVLEN VLENGIEHTT SHPPQVHITT TKHTPNSRIE LIVTDNGPGI
     PTHERTAVLD GTVSATTHSS GLGLWLIKWG IDRLGGTFTI EQCDDPGCGT RVRIRLRTEL
     EQE
//
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