ID   Q2FN62_METHJ            Unreviewed;      1009 AA.
AC   Q2FN62;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer with Pas/Pac sensor {ECO:0000313|EMBL:ABD39795.1};
GN   OrderedLocusNames=Mhun_0016 {ECO:0000313|EMBL:ABD39795.1};
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:ABD39795.1, 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; ABD39795.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2FN62; -.
DR   STRING; 323259.Mhun_0016; -.
DR   EnsemblBacteria; ABD39795; ABD39795; Mhun_0016.
DR   KEGG; mhu:Mhun_0016; -.
DR   eggNOG; arCOG02318; Archaea.
DR   eggNOG; arCOG02320; Archaea.
DR   HOGENOM; CLU_000445_107_20_2; -.
DR   InParanoid; Q2FN62; -.
DR   Proteomes; UP000001941; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd11386; MCP_signal; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.20.120.1530; -; 3.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF18947; HAMP_2; 6.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 5.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 4.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001941};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284}.
FT   DOMAIN          1..31
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          144..196
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          235..287
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          326..378
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          417..469
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          719..955
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   1009 AA;  108343 MW;  E3CD7930BC433284 CRC64;
     MPIFEINPDL SIAKINSACS QVTGYSTEQL LKMNLSELTV TKRTGRTARD AIEMKTVLSG
     ELELDVPAGQ KVLEYLYLPI LDDNGDVLSV ISFYVDKTAE KTAVRDIISL TQAAKAGQLD
     TRVDPDKYEG DLLLLAKGIN ATLDAVIGPL NVAAEYVDRI SKGDIPPKIT DSYNGDFNEI
     KNNLNQCIDA VNCLIADAGM LSRAAVEGKL DTRADATKHQ GDFRKIVEGV NATLDAVIGP
     LNVAAEYVDR ISKGDIPPKI TDSYNGDFNE IKNNLNQCID AVNYLIADAG MLSRAAVEGK
     LDTRADATKH QGDFRKIVEG VNATLDAVIG PLNVAAEYVD RISKGDIPPK ITDSYNGDFN
     EIKNNLNQCI DAVNYLIADA GMLSRAAVEG KLDTRADATK HQGDFRKIVE GVNATLDAVI
     GPLNVAAEYV DRISKGDIPP KITDSYNGDF NEIKNNLNQC IDAVNYLIAD AGMLSRAAVE
     GKLDTRADAT KHQGDFRKIV EGVNATLDAV IGPLNVAADY VDRISKGDIP PKITDSYNGD
     FNEIKNNLNQ CIDAVNCLIA DAGMLSRAAV EGKLDTRADA TKHQGDFRKI VEGVNATLDA
     VIGPVKEAMR VAERYAKADF STRVDENLHV AGDFVLFKNS LNNIGIFVQS AIQEIQRISN
     LYASGNFAAE FDRNLKIEGD LALLRDALDT IGMNVSEVLS VIAREMKQLA HQAETAGTGI
     EDLSRGAELI AKNADQTKQN AERSEDGINQ VLQTMEDLTR TISEVSSNAE RVAGLSVQAN
     DLAKQGIGAA GKADKGMQSI TKTSEEVETI FAEIRAQMHE IVKIVDLITD IANQTNLLSL
     NAAIEAARAG EAGKGFAVVA AEVKSLAQRS RQSAEHIADM ISDLQKKSDA ASGAMAEAGT
     AVAEGSAALS ETLGIFNTLT TSVEDITRNM EMVASATEEQ AASFEEITAS VNEMSLLVKD
     TAKDALNSSA TSEEALAVVD QITNVISQIN EVVKTIGTEM DKFTYKNKS
//