ID Q2W3W1_MAGSA Unreviewed; 621 AA. AC Q2W3W1; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 92. DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:BAE51464.1}; GN OrderedLocusNames=amb2660 {ECO:0000313|EMBL:BAE51464.1}; OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Magnetospirillaceae; Paramagnetospirillum. OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE51464.1, ECO:0000313|Proteomes:UP000007058}; RN [1] {ECO:0000313|EMBL:BAE51464.1, ECO:0000313|Proteomes:UP000007058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058}; RX PubMed=16303747; DOI=10.1093/dnares/dsi002; RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.; RT "Complete genome sequence of the facultative anaerobic magnetotactic RT bacterium Magnetospirillum sp. strain AMB-1."; RL DNA Res. 12:157-166(2005). 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; AP007255; BAE51464.1; -; Genomic_DNA. DR RefSeq; WP_011385040.1; NC_007626.1. DR AlphaFoldDB; Q2W3W1; -. DR STRING; 342108.amb2660; -. DR KEGG; mag:amb2660; -. DR HOGENOM; CLU_000445_107_27_5; -. DR Proteomes; UP000007058; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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; cd06225; HAMP; 1. DR Gene3D; 6.10.340.10; -; 1. 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; IPR004089; MCPsignal_dom. DR InterPro; IPR000727; T_SNARE_dom. DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1. DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF00015; MCPsignal; 1. DR PRINTS; PR00260; CHEMTRNSDUCR. DR SMART; SM00304; HAMP; 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; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS50192; T_SNARE; 1. PE 3: Inferred from homology; KW Methylation {ECO:0000256|ARBA:ARBA00022481}; KW Reference proteome {ECO:0000313|Proteomes:UP000007058}; KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE- KW ProRule:PRU00284}. FT DOMAIN 210..263 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 303..528 FT /note="Methyl-accepting transducer" FT /evidence="ECO:0000259|PROSITE:PS50111" FT DOMAIN 455..517 FT /note="T-SNARE coiled-coil homology" FT /evidence="ECO:0000259|PROSITE:PS50192" FT REGION 562..621 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 621 AA; 66375 MW; 79C4700E74311138 CRC64; MLARVADARI TVKFFIAPLL LVACIMVLGA VFHVAMERQE QSMEGMVTVS FANSRTAAEL DGMAATIESN IYRLLGWQAA KEEKDRIRAL DTQVRADLKT LGEKSKALLD SLKAEPATSK QIRDYILAAG DVLDMYQSDH VTALAMMGAT ELEYDGIRAK LREMTTKAAA SAAEDYHEAK ASADSTRTQY FLVLAIFLAL GVVVTLGMAR LTARPVTQLT GIMGRLAEGS TDVEIPSQDG RDEVGEMARA VAVFRDGMKR AADLESQQRR QREQQTELLA RRDRMIAEFN GAMEKIMATV SSSIERVHTL SSSLQSTAEQ TSAQGSAVAG AAEHSAANVA TVASAAEQLG SSVQEISRRV TETATITSEA VSGIHTANTT MDGLAEAARR IGEVVQLIND IAGQTNLLAL NATIEAARAG EAGKGFAVVA SEVKTLANQT ARATDEIAQQ IAGIQSISQE AVQTIRNVGT TIDRVNEVVS SIAAAVEEQS AATDEIVRSV QEASSGNAEI TRNIADVSKA ATATGEMASG MFKAADELVE EAGHLRSEVS GFLGNMRQRI RHEKSRTRHH RPRSGSHHAD LIPSCGDRNR SPQRPHAAGG RRAPLPPARK ARGPLGLTNP R //