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Database: UniProt
Entry: Q8PU38_METMA
LinkDB: Q8PU38_METMA
Original site: Q8PU38_METMA 
ID   Q8PU38_METMA            Unreviewed;       702 AA.
AC   Q8PU38;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   SubName: Full=Sensory transduction histidine kinases {ECO:0000313|EMBL:AAM32214.1};
GN   OrderedLocusNames=MM_2518 {ECO:0000313|EMBL:AAM32214.1};
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM32214.1, ECO:0000313|Proteomes:UP000000595};
RN   [1] {ECO:0000313|EMBL:AAM32214.1, ECO:0000313|Proteomes:UP000000595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC   {ECO:0000313|Proteomes:UP000000595};
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA   Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA   Fritz H.J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR   EMBL; AE008384; AAM32214.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8PU38; -.
DR   KEGG; mma:MM_2518; -.
DR   PATRIC; fig|192952.21.peg.2883; -.
DR   eggNOG; arCOG02376; Archaea.
DR   HOGENOM; CLU_000445_114_71_2; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
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; 3.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
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); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AAM32214.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:AAM32214.1}.
FT   DOMAIN          1..66
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          78..144
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          201..244
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          273..323
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          324..394
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          465..684
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          307..334
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   702 AA;  78462 MW;  DA07E1E052081CF6 CRC64;
     MLPECDGYEI CRILKNDPDY KFIPIIVISG FFEKPNKLKA TRCGADDFIQ KPIDRFELKT
     RIKSLIRIKK NYEALQESES RYRQFFNNSP AVTLLVDPES YRIVDANDPA CAYYGYTYEE
     MTAKKISDIN VFSEEKNKEI TRQVFLEKRG HFYSCHKLAS GEIRHVEVYI NTVNIRDKEL
     FFINVYDITA SKKAERELIE SEEKFKQVVE LSVDGIIIGT DSGKIVDCNG AACRIFGYDK
     EEILKLQVID LFPGDLNIIA HDITSCNKAA GEKTVERINQ KKDGTSFPAE VAARRVKLGN
     EEGLIVYVRD ITERKKAEKA LKESEENFRT LVNNTLDGIL ILDFEGRVLA ANAAIGKMLG
     MELEKVAGID IMKYLAPESV PVAVEDQINV LNGRGGYLSV YKSTSCNGEP LWIEGLGTKI
     IYRGQPANIV VIRDITARKK AEEALINAKT AAEAANRTKS EFLTNMSHEL KTPLNSIIGF
     SDLLIEGIAG PLNEKQSRYA GFISSNGKNL LNIINGILEL SKVESEGDEL TLQEFSVNES
     INKSISTALP QILKKNIKLN YNSDSDPLCI FADENKFRQI MESLLNNAVK FTPEDGLIDI
     SSKQEGGIVT IKVKDTGIGI PEDSLDKIFK PFIQLESSLS RTFEGTGLGL TLAKKYVEMH
     GGNISVESKT GKGSSFKVEL PVNRQKTVRT TIQKLDQQIV ES
//
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