ID   Q2W6B5_MAGSA            Unreviewed;       575 AA.
AC   Q2W6B5;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:BAE50610.1};
GN   OrderedLocusNames=amb1806 {ECO:0000313|EMBL:BAE50610.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE50610.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE50610.1, 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}.
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DR   EMBL; AP007255; BAE50610.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W6B5; -.
DR   STRING; 342108.amb1806; -.
DR   KEGG; mag:amb1806; -.
DR   HOGENOM; CLU_000445_107_27_5; -.
DR   Proteomes; UP000007058; 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   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; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF12729; 4HB_MCP_1; 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.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007058};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          226..279
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          319..541
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   575 AA;  60726 MW;  17E444D1037BBD16 CRC64;
     MGQSGPNFTY LRRTNSMLDR LSVAKKLILS FGAILSVVIG LSVFAVNRLA AVNQLSTDLA
     DNWLPSVDVS RELDGLLAKQ RATVFRHILT TDEAQMAEVE KVLNDQHSAF VAALERYGKL
     LSSPEEKANF DDWAKVAVEY DAMTARALDF SRKNENDKAK EVILSNLPLY ANAQKHAAKA
     VEINVRGGKD ASLAGDALYH LSRMILLIAV AVVIVMVVIF GLLLRKSIAE PIIAMTAAMN
     RLADKDFAVA IPAVGRVDEV GRMASAMQTF KDNMLRSEQM ESEQRAAQER NVARGKTIES
     LTRNFDEAVS SMLNAVSRAS TDMEHAAQGM SATAEQTSRQ AVMVAAATEE ASSSVQTVAS
     AAEELAASIH EIGRQVTQSS TVARMAAEEA SKTNQTVNGL AESSARIGDV VSLINDIASQ
     TNLLALNATI EAARAGDAGK GFAVVAGEVK NLANQTGRAT EEISQQIAAV QEATRQAVDA
     IGGIVKRIEE INQISAAIAS AVEEQSAATA EIARNVQQAA SGTQEVSATI GGVTKAAEET
     GTAAVGVLGS IKSVNQQADA LKGVVANFLT GVKSA
//