ID A1ASJ2_PELPD Unreviewed; 969 AA. AC A1ASJ2; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 79. DE SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ABL00313.1}; GN OrderedLocusNames=Ppro_2710 {ECO:0000313|EMBL:ABL00313.1}; OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales; OC Desulfuromonadaceae; Pelobacter. OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABL00313.1, ECO:0000313|Proteomes:UP000006732}; RN [1] {ECO:0000313|EMBL:ABL00313.1, 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}. 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; CP000482; ABL00313.1; -; Genomic_DNA. DR AlphaFoldDB; A1ASJ2; -. DR STRING; 338966.Ppro_2710; -. DR KEGG; ppd:Ppro_2710; -. DR eggNOG; COG0840; Bacteria. DR HOGENOM; CLU_000445_107_20_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; cd19411; MCP2201-like_sensor; 1. DR Gene3D; 1.20.120.1530; -; 2. DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1. DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR024478; HlyB_4HB_MCP. DR InterPro; IPR004089; MCPsignal_dom. DR InterPro; IPR047347; YvaQ-like_sensor. DR PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1. DR PANTHER; PTHR43531; PROTEIN ICFG; 1. DR Pfam; PF12729; 4HB_MCP_1; 1. DR Pfam; PF18947; HAMP_2; 2. DR Pfam; PF00015; MCPsignal; 1. DR PRINTS; PR00260; CHEMTRNSDUCR. DR SMART; SM00304; HAMP; 3. 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 13..32 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 192..216 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 307..359 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 487..539 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 672..887 FT /note="Methyl-accepting transducer" FT /evidence="ECO:0000259|PROSITE:PS50111" FT REGION 683..717 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 858..885 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 969 AA; 104503 MW; 2BBF6BB12A36FF83 CRC64; MNWFNNMTLK AKLMTGFVCV AVIASLIGLI GIREIRVIKR ADTTLFEKAA VPMGELADFA IAFQQIKVNV RDILMASSVE EKKRYAERIK ELRTSLNEKA DAFEKTILSE EGRSLFDDFK AARKAFGADL DRIIELSLQN RNAEALELLR GAADRSSGAE QSAIEKLMDA KIKQAKLIAD DNDSIAGSAS RIMLALMVVG TLVAIGLGFL LTRFILGQLG GDPSRVAEIA NRVAAGDMSL EIDLTGKNGD SVMSSMAKMV DSIKLLVADA ALLSDAAIAG QLATRADAGR HRGDFRKIIA GVNDTLDAVI GPLNVAAEYV DRIGKGDIPP RITDNYSGDF NEIKVNLNLC IDGLQGLVEA NQVLQRVALN DYTRRVEGSY QGIFAQVAAA TNATIGRVTS VLGICQHIAR GEYTEDLEAL RKIGKRCEND TLMPAFITMM ESIDALVSDA TMLSRAAVAG NLATRADASR HQGDFRKIIT GVNDTLDAVI GPLNVAAEYV DRIGKGDIPP RITDNYSGDF NEIKVNLNLC IDGLQGLVEA NQVLQRVALN DYTRRVEGSY QGIFAEVASA TNAARDRVMR ARDICQHIAR GEYKDDLEAL KKIGKRCEND TLIPALITMC ESIDDITANA KQVAQGNLMV EMKKRSENDE LMESLASMVA KLREIVMEVQ SAVDNVASGG QQMSATAQQM SQGASEQAAS AEEISSSMEE MASSIRQNTD NALQTEKIAI KSASDAREGG KAVTETVAAM KEIATKISII EEIARQTNLL ALNAAIEAAR AGEHGKGFAV VASEVRKLAE RSHTAAGEIG QLSASSVAIA EQAGEMLSRM LPEIQRTAEL VQEIAASSRE QDSGADQINK AIHQLDQVIQ QNASASEEMA STTEELSSQA EQLKATIAFF ALDDRKQKAL PGPRHGAPKQ IAAGLVRQAI AMRTSTQNGK TPSRTQCEGV HLHLDHEGVD AMDSEFERF //