ID   Q2FMR5_METHJ            Unreviewed;       933 AA.
AC   Q2FMR5;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer with Pas/Pac sensor {ECO:0000313|EMBL:ABD40261.1};
GN   OrderedLocusNames=Mhun_0499 {ECO:0000313|EMBL:ABD40261.1};
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD40261.1, ECO:0000313|Proteomes:UP000001941};
RN   [1] {ECO:0000313|Proteomes:UP000001941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC   {ECO:0000313|Proteomes:UP000001941};
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000254; ABD40261.1; -; Genomic_DNA.
DR   RefSeq; WP_011447548.1; NC_007796.1.
DR   AlphaFoldDB; Q2FMR5; -.
DR   STRING; 323259.Mhun_0499; -.
DR   EnsemblBacteria; ABD40261; ABD40261; Mhun_0499.
DR   GeneID; 25393445; -.
DR   KEGG; mhu:Mhun_0499; -.
DR   eggNOG; arCOG02318; Archaea.
DR   HOGENOM; CLU_000445_107_18_2; -.
DR   InParanoid; Q2FMR5; -.
DR   OrthoDB; 8523at2157; -.
DR   Proteomes; UP000001941; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd11386; MCP_signal; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_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; IPR013767; PAS_fold.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   SMART; SM00283; MA; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001941};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}.
FT   DOMAIN          49..94
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          115..167
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          445..488
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          576..628
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          647..883
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   933 AA;  105058 MW;  B04B8326F2ABD9CE CRC64;
     MTDQLRDILI HILSDDPSPD IPGTDILPGE GDRELLTSFV QKRAVLQKKK NRMDAIFAHS
     PQPILILNPE ARITEVNPSF LQISGFSPEA CIGKPIQTIV PGFVLPGHGY NESRRDSEIF
     TLDFPHGRRI LEQYPIPVRD ESGTLTEIIL VFKDITIRVQ AEQKAEEIRE KLAHDYGERV
     KEQKVFYSVA SLIQEDTLSV PDVLSKVAFL IPPGWQYPEE TVARILYGNE VYTTPDFIET
     PWIQRALFQT RRGTEGIIEV AYLSEKAPEY EGPFLLEERN LINSLAEMLK TYIDRKEGEQ
     ELEKKMHDLG ERVKEQQLFY KTSSLIQDDS KKITEVLQDV VLLLPPGWQY PEITGGRIQY
     GDTALATPNF RESPWIQTSS FITRAGMTGK IDVVYLEEKP PEYEGPFLKE ERNLINSLAD
     MLKTYIDRKE GEQELERRMM EIEELEHLNN TIVQQIPMPV LLIDENQQIL VTNDAYIRLT
     GYTREELLHM TPRDITVLEY SGEGLKELLS TMKPTFGELT CKFPLGIRIL EQYGIPIFSR
     SGLLENYLIV YNDITERKRQ EEEVQKLLTD SRTMSETLSK SAEDLETGMA RMAEGDLRYR
     APVMEQDPLS KIKNDYNTAL AAISLLIEEL EGSISLLTGT SEKTLSQTDN IKKAIRDIAD
     DVQNSTAGAR EQMEETRRIS DDIRLLSERI SQIVDITTRL MELAAQTASQ GVEAGQIGGV
     ASEKMESVGK ISADNMKQIT GLNEQMAEID KIVRLISDIS SQTNLLALNA AIEAARAGEH
     GRGFAVVAQE VKNLAGQSKL ATTQIEELIR TIQSKSADTV TSIEAAYKEI HEGIASVNKT
     IDVLSSITSH VTEISDGISQ VMVATKDEEV LMNRVQEGIG VMNSESEKNL ARMEEISHRM
     DESRHATDDI ASSSLEIARL SGNLKKQADR FFL
//