ID MCP25_MAGSA Reviewed; 576 AA. AC Q2W4T8; DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=Methyl-accepting chemotaxis protein Amb2333 {ECO:0000303|PubMed:20471399}; GN OrderedLocusNames=amb2333; OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Magnetospirillaceae; Paramagnetospirillum. OX NCBI_TaxID=342108; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMB-1 / ATCC 700264; 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). RN [2] RP SUBCELLULAR LOCATION, AND POSSIBLE METHYLATION AT GLU-365. RC STRAIN=AMB-1 / ATCC 700264; RX PubMed=20471399; DOI=10.1016/j.jmb.2010.05.011; RA Philippe N., Wu L.F.; RT "An MCP-like protein interacts with the MamK cytoskeleton and is involved RT in magnetotaxis in Magnetospirillum magneticum AMB-1."; RL J. Mol. Biol. 400:309-322(2010). CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the CC concentration of attractants and repellents in the environment, CC transduce a signal from the outside to the inside of the cell, and CC facilitate sensory adaptation through variation of methylation levels. CC Attractants increase the level of methylation while repellents decrease CC the level of methylation. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:20471399}; Multi-pass membrane protein CC {ECO:0000255}. Note=Found predominantly at cell poles. CC {ECO:0000269|PubMed:20471399}. CC -!- MISCELLANEOUS: There are over 60 methyl-accepting chemotaxis proteins CC in this bacterium. {ECO:0000269|PubMed:16303747}. CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein CC family. {ECO:0000305}. 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; BAE51137.1; -; Genomic_DNA. DR AlphaFoldDB; Q2W4T8; -. DR SMR; Q2W4T8; -. DR STRING; 342108.amb2333; -. DR KEGG; mag:amb2333; -. DR HOGENOM; CLU_000445_107_21_5; -. DR Proteomes; UP000007058; Chromosome. DR GO; GO:0060187; C:cell pole; IDA:UniProtKB. 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:UniProtKB-KW. 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 Gene3D; 3.30.450.20; PAS domain; 1. DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt. DR InterPro; IPR004010; Double_Cache_2. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR004089; MCPsignal_dom. DR InterPro; IPR033480; sCache_2. 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; PF08269; dCache_2; 1. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF00015; MCPsignal; 1. DR PRINTS; PR00260; CHEMTRNSDUCR. DR SMART; SM01049; Cache_2; 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. PE 1: Evidence at protein level; KW Biomineralization; Cell inner membrane; Cell membrane; Chemotaxis; KW Membrane; Methylation; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..576 FT /note="Methyl-accepting chemotaxis protein Amb2333" FT /id="PRO_0000447749" FT TRANSMEM 26..46 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 204..224 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 226..279 FT /note="HAMP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102" FT DOMAIN 320..556 FT /note="Methyl-accepting transducer" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284" FT REGION 279..299 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 279..295 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 351 FT /note="Glutamate methyl ester (Gln)" FT /evidence="ECO:0000250|UniProtKB:P02942" FT MOD_RES 365 FT /note="Glutamate methyl ester (Glu)" FT /evidence="ECO:0000305|PubMed:20471399" FT MOD_RES 547 FT /note="Glutamate methyl ester (Glu)" FT /evidence="ECO:0000250|UniProtKB:P02942" SQ SEQUENCE 576 AA; 61358 MW; F4D0A3F6E805A284 CRC64; MEGPYQRLPW GIWRMSISNW RFRAKIFLIV VLSLLGMGAI VAVNLANLHN ELMAARKIKT QHVVETAHSL IGHYVKLSQS GQMSTDAAQA AAIEAIKTMR YAGTEYFWIN SLAGKMVVHP IRPDMLGKDL MGLKDPAGKL FFEAMIDVVK KDKAGFVDYL WPKPGLDQPV PKVSYVKGIE EWGWLVGSGI YVDDVDSAFR AEVMNLGGIV TGVVLLVLLV SWWIGKNVVD GMRNATGGIR KLAEGDTSVE IKGHERGDEI GELVQAAEIF REHSLTMKRM SEERAEQRRQ AEAERRSTLA GLATELERGV KSTVVTVSES AGRMRSTATG MAGAIDNASQ ESQAVAAAAQ QTSSNVEAVA AAAEELSSSI RGIGSQVAES TQIAKEAVDA ANRTDGVVRG LSEAADRIGE VVRLINDIAG QTNLLALNAT IEAARAGEAG KGFAVVANEV KHLASQTAKA TEEIGQQIAS IQSTTADAVG AIESIGKTIG RMDEIANAIA EAVEQQGAAT QEIARNVHEA ADGAQEVSHH ISSISRTASE AGVAARELLG AAAELAGESE TLRNGVDRFL GEVRAM //