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Database: UniProt
Entry: Q2W5W2_MAGSA
LinkDB: Q2W5W2_MAGSA
Original site: Q2W5W2_MAGSA 
ID   Q2W5W2_MAGSA            Unreviewed;       535 AA.
AC   Q2W5W2;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:BAE50763.1};
GN   OrderedLocusNames=amb1959 {ECO:0000313|EMBL:BAE50763.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE50763.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE50763.1, 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; BAE50763.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W5W2; -.
DR   STRING; 342108.amb1959; -.
DR   KEGG; mag:amb1959; -.
DR   HOGENOM; CLU_000445_107_27_5; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0016020; C:membrane; 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   InterPro; IPR003660; HAMP_dom.
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; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
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   Coiled coil {ECO:0000256|SAM:Coils}; 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        163..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          185..238
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          272..508
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          229..256
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   535 AA;  55719 MW;  9E401B0325F59F5D CRC64;
     MQGLAGQSRT LDEIAEVSFA KSVKIGDFTD VLQDAHSDLY RLLTWNAAGV EAAKVDKIEG
     AFADGLKKAK KQLGDYRSAF AVTAEEDALL KKIDAGLGVY KNATDQVVAM QKMDFTAAVS
     FMWTAQDSYQ ALMAETQAMV ALEARMVEAA RQSASQDAGT TRGLFIGITL GVLGLLALIS
     FLLVRAIASA VGGMTGAMER LAQGDLGVVV PAIGRRDEIG AMAAAVQVFK DNAQRVKNLT
     DEQEALQRQA EAAKRQAMTD LAGEIETTVR GAVENASRAA DSIRGEAEVL AANAETAISQ
     TAQVAESSEL ANGNVETVAQ AASRLVGSIS EINRQVEESS RVASEAVAEA ARTDETVKTL
     TVASGKIGEV VNLINDIASQ TNLLALNATI EAARAGDAGK GFAVVANEVK NLANQTARAT
     EEITGEITAM KAATEEAVRA IDGIVATIGR VNEALAAITG AVAEQGRATS EISDSVSQAA
     DGTRTVSSGI GEVRRVADQV GNAAATVQVT TETLVGEFDR LQTQVDGLVV RLKSA
//
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