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   25-MAY-2022, entry version 92.
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; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
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}.
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DR   EMBL; AP007255; BAE51137.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W4T8; -.
DR   SMR; Q2W4T8; -.
DR   STRING; 342108.amb2333; -.
DR   EnsemblBacteria; BAE51137; BAE51137; amb2333.
DR   KEGG; mag:amb2333; -.
DR   HOGENOM; CLU_000445_107_21_5; -.
DR   OMA; ENITHTI; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0060187; C:cell pole; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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   Pfam; PF08269; dCache_2; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM01049; Cache_2; 1.
DR   SMART; SM00283; MA; 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