ID Q2WAS6_MAGSA Unreviewed; 561 AA.
AC Q2WAS6;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:BAE49049.1};
GN OrderedLocusNames=amb0245 {ECO:0000313|EMBL:BAE49049.1};
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE49049.1, ECO:0000313|Proteomes:UP000007058};
RN [1] {ECO:0000313|EMBL:BAE49049.1, 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; BAE49049.1; -; Genomic_DNA.
DR RefSeq; WP_011382692.1; NC_007626.1.
DR AlphaFoldDB; Q2WAS6; -.
DR STRING; 342108.amb0245; -.
DR KEGG; mag:amb0245; -.
DR HOGENOM; CLU_000445_107_27_5; -.
DR OrthoDB; 3378718at2; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 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 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; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 306..542
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 468..520
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
SQ SEQUENCE 561 AA; 58546 MW; 8FBC919B890C59A8 CRC64;
MPSVATIRGK LTALAVTVAV VLGGLSLGWG VVLSELKVNG PVYGRIVQAK DLVADILPPP
EYIIESYLVA SQALAAEPSK LAPLKEAMIR LRRDYDDRHQ YWQGQDLEAS VRDGLLVESY
KPAVQFFDHA FSTYFPALEK GDREAARASF AVLGGLYATH RAAIDTLVTR SDALSKAVEA
QAAASESSYK LLVIVLTLAS ALAALALVIG MSRAIVAPMA RLGEAVGRLG GGALDAGVPE
TERVDEIGPL ARALDGWRQG LIAAEARRRD EAEEQSRLQA RQRRVEAATR RFDEAIITML
ARIRDSAENL HAASNSLSAN AEQTHAQGAA VSAATEQSAA SVESVASAGN QLSSSIEEIS
SQVRQSSAIV AAASHEAEAA NGRIAGLTEA VERIGQVLSL INDIASQTNL LALNATIESA
RAGEAGKGFA VVAHEVKNLA GQTSRATEDI ARQIAAVRDE AGTAVAALAG IAQTIARINE
MSASIAGAVE QQGAAASEIS RNVEQAAAGS REVVHNITGV VGAAGETGAM ARNVFAAANQ
LLGQSTELER EVAAFLREMA A
//
