ID   A1APE6_PELPD            Unreviewed;      1500 AA.
AC   A1APE6;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ABK99216.1};
GN   OrderedLocusNames=Ppro_1601 {ECO:0000313|EMBL:ABK99216.1};
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK99216.1, ECO:0000313|Proteomes:UP000006732};
RN   [1] {ECO:0000313|EMBL:ABK99216.1, ECO:0000313|Proteomes:UP000006732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC   {ECO:0000313|Proteomes:UP000006732};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000482; ABK99216.1; -; Genomic_DNA.
DR   STRING; 338966.Ppro_1601; -.
DR   KEGG; ppd:Ppro_1601; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_248706_0_0_7; -.
DR   Proteomes; UP000006732; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Gene3D; 1.20.120.1530; -; 6.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF18947; HAMP_2; 6.
DR   Pfam; PF00015; MCPsignal; 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   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        51..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          119..176
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          1109..1161
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          1205..1420
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          1216..1252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1442..1500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1391..1418
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1500 AA;  162690 MW;  965D61A67D596B51 CRC64;
     MKTMAKENKN MFKDTGLKKM LMSGFIAMAL IGGILGGVGA KLALGSTSGS APLFVLALVA
     VGVVLAIVLG SSIVRAVLGQ LGAETGEVAA IANLLASGDL SRDIQVAPGD STSVMAALKR
     VSDSVRSVVS DASTLSDAAI AGKLSVRADA ARHTGEFRRI VEGVNGTLEA VVETVHDAAK
     RIDLLSRGEI FEEITDGYRG DFGELRESLN RCKQANEALR VDIRTMCIAS YEGHLDTRVD
     PDKHQGFFSR AVAGLNNLFE NFTAPLKVTT DYIETISHGA LPEVITEEYR GDYNNIKQSV
     NRCIEGLGGL VEANNVLQKM AVNDHTQKVE GQYLGIYAEV GHAVNDVRER LLRVAQTARS
     IACGDTSDLE IYKAIGDGKG RRSENDHLVP NFIGMMEAIN ALVSDANMLA DAAVHGNFNT
     RADLSKHQGD FRKIVAGVNA TLDTVVDKVV WYEAIIDAVP FPIHVIDMDM NWTMLNKAFE
     KLMIESGAVP DRRAAVGKPC SSAAANICNS EKCGIRQLQK GVGESFFDWH GAHCKQDTSY
     LLNKNGEKIG YVEVVTDLTP ILRNRDYTHA EIERMADNLT RLASGNLELD LQVKEADEHT
     VATREDFVKI NESLARVKEA VGSMIADTDM LVHEAIAGRL ETRADADKHQ GEYRKIVAGI
     NQTLDTVVDK VVWYEAIIDA VPFPIHVIDM DMNWTMLNKA FEKLMIESGA VPDRRAAVGK
     PCSSAAANIC NSEKCGIRQL QRGIGESYFD WHGSQCKQDT SYLVNKRGEK IGYVEVVTDL
     TPILRNRDYT NCEIERMADN LTRLSAGNLE LDLQVKEADE HTAATREGFV KINDSLTKVK
     EAVGSMIADT DMLVHEAIAG RLETRADADK HQGDYRKIVA GINQTLDTVV DKVMWYEAII
     DAVPYPLHVI DMDMNWTMLN KAFEKLMIDS GAVPDRRAAV GKPCSSAAAN ICNTEKCGIR
     QLQKGVGESY FDWHGSQCKQ DTSYLLNKKG EKIGYVEVVS DLTPILRNRD YTNCEIERMA
     ENLTRLSAGN LELDLQVKEA DEHTAATREG FVKINDSLTK VKEAVGSMIG DTNLLVNAAL
     EGRLATRADA GKHQGDFQKV VSGINSTLDA VIGPLNMAAD YVARISRGDM PSAISDTYNG
     DFNDIKNNLN VLIDAIGDIT ANAKQIAQGN LMVDLKKRCE DDELMESLAS MVEKLREVVT
     EVQSAADNVA AGGQQMSATA QQMSQGATEQ AASAEEVSSS MEEMASSIRQ NTDNALQTEK
     IAIKSASDAR EGGRAVTETV SAMKEIATKI SIIEEIARQT NLLALNAAIE AARAGEHGKG
     FAVVASEVRK LAERSQAAAG EISQLSTTSV AIAEQAGEML DKMLPDIQKT AELVQEISAA
     SREQDSGAEQ INKAIQQLDQ VIQQNASASE QMASTTEELS SQAEQMKATI AFFALDDRRQ
     KALPGPRNAA PRQITAGPRR QAPVVKKPAM PPARSPKSGG VNLDLGPIGP DSLDNEFEKF
//