ID   Q46DT3_METBF            Unreviewed;       689 AA.
AC   Q46DT3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAZ69959.1};
GN   OrderedLocusNames=Mbar_A0989 {ECO:0000313|EMBL:AAZ69959.1};
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ69959.1};
RN   [1] {ECO:0000313|EMBL:AAZ69959.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Fusaro {ECO:0000313|EMBL:AAZ69959.1};
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   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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; AAZ69959.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46DT3; -.
DR   STRING; 269797.Mbar_A0989; -.
DR   PaxDb; 269797-Mbar_A0989; -.
DR   KEGG; mba:Mbar_A0989; -.
DR   eggNOG; arCOG02344; Archaea.
DR   HOGENOM; CLU_000445_107_19_2; -.
DR   OrthoDB; 8523at2157; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR032255; HBM.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM01358; HBM; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS51753; HBM; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..293
FT                   /note="HBM"
FT                   /evidence="ECO:0000259|PROSITE:PS51753"
FT   DOMAIN          320..372
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          382..444
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   DOMAIN          391..627
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          630..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  75874 MW;  E8FF0F3371EF8176 CRC64;
     MYKNTKIGHL VIGFALLLIL IFFVGYTGYQ GMNDVEKKSR AIQNMTFITN NMQGALEAQE
     SYVIYGDPVY KEDTYTHLDL VPTQAAISKE IYLGYLDPVN QDRMDSILKT SGEFRESFDS
     YVKADDEEIA LRTNITSKGD LILKKADELY QDQMFQYQQY LENGSSGEVL QQKLSNAQEA
     QKISILAMEA RNQYQNYIIT PEDQYAENFD RIMENITEVT ESLNKQMVKP ENLELGNTII
     ASVTEIRSDF DSLTVLKEKK AADVKNMATI AAQINKTAEA ASADQKEKLD TLIVNSISKI
     FLVTLLSILI GALLVFVILN LYRKPIYELL EAAEKISNGD LSVEIEGNSR SEISQLSQAF
     KSMVENLRGL IQGIQESSVH LSTLSEEMSA SSEEVASASR KISDTATEIS NGTEVQSTKI
     VDITHAMQDM THNIQEIADN TQKVSKNTNL VNNTINSIGN ASRELLVKMN HIRFSVDETK
     EVITELDSKS QQINEIVTLI TRIADQTNML ALNAAIEAAR AGEHGRGFSV VADEVRKLAD
     ESGRAANNIS SLIDEIRGSI SETVESIEAS KKDVQAGSLS VNNAVEMVSG IVTTINEITN
     MIEDVAAATE EQSASIEEIT STLEDISSIS EQSTAGTQET AAALEEQSAS MSELANMASD
     LSLLGERMKK ATEKFKLSNL KEGSENKSS
//