ID Q46BW3_METBF Unreviewed; 565 AA.
AC Q46BW3;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Signal-transducing histidine kinase {ECO:0000313|EMBL:AAZ70629.1};
GN OrderedLocusNames=Mbar_A1687 {ECO:0000313|EMBL:AAZ70629.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ70629.1};
RN [1] {ECO:0000313|EMBL:AAZ70629.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fusaro {ECO:0000313|EMBL:AAZ70629.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Goodwin L.A., Saunders E.H., Schmutz J.,
RA Larimer F., Land M., Anderson I., Richardson P.;
RT "Complete sequence of chromosome 1 of Methanosarcina barkeri str. fusaro.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000099; AAZ70629.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46BW3; -.
DR STRING; 269797.Mbar_A1687; -.
DR PaxDb; 269797-Mbar_A1687; -.
DR KEGG; mba:Mbar_A1687; -.
DR eggNOG; arCOG02327; Archaea.
DR HOGENOM; CLU_000445_114_58_2; -.
DR OrthoDB; 8127at2157; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR031621; HisKA_7TM.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF16927; HisKA_7TM; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AAZ70629.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:AAZ70629.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..283
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 357..558
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 565 AA; 64341 MW; 0BCF45D4F97ACC67 CRC64;
MGALIFSGVM STLLAIKAYK AFQYRRMYFS KYFILIMLSM SLWSVNYAFE VGFMDIELKY
LFARLEYIGM AFAPVAWFLF ASEYSGICKE FIRKYQNEFF IMPLFIILLM LTNSFHGMYF
LGYYLDISKG FPLLVLIHGP FFWVFYIYSF ILIFLGIFFF FNQFVHLTAP YRAQAAIALT
AACIPVLGNI LHIANIGPFS FLDPTPFAFT ITGLILFWGI MQHEFLNIIP IARENVIESM
SDGYIVVDLA DSIVDINKAA LELAGKTKKE VLGRNLNELF GNEVQMPQSE AHESNFHKEI
FLKSGLETKL FTLSVSPLLT KDDEEGRLLM MHDTTETYRY QEALKQANKK INLMSNITRH
DILNQVNVLS GYTELISETL PENVKNDPRI VKYLNNLNKG IETIHSQIVF TKDYQELGVV
SPIWQSVSNT AREASFPFSG QSLKFSIEES RVEIYADPLL KKAFYNLFDN AGSHGEHVTE
ISVSSRRTDD NLIIEIKDNG IGISPEMKEL IFQKSIGKNT GLGLFLVKGI LSITDMEIKE
TGTEGTGARF EITVPLGNWR ENTSQ
//
