ID M1Q576_BACTU Unreviewed; 575 AA.
AC M1Q576;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AGF99786.1};
GN ORFNames=H175_ch1074 {ECO:0000313|EMBL:AGF99786.1};
OS Bacillus thuringiensis serovar thuringiensis str. IS5056.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1286404 {ECO:0000313|EMBL:AGF99786.1, ECO:0000313|Proteomes:UP000011719};
RN [1] {ECO:0000313|EMBL:AGF99786.1, ECO:0000313|Proteomes:UP000011719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS5056 {ECO:0000313|EMBL:AGF99786.1};
RX PubMed=23516221;
RA Murawska E., Fiedoruk K., Bideshi D.K., Swiecicka I.;
RT "Complete genome sequence of Bacillus thuringiensis subsp. thuringiensis
RT strain IS5056, an isolate highly toxic to Trichoplusia ni.";
RL Genome Announc. 1:E0010813-E0010813(2013).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP004123; AGF99786.1; -; Genomic_DNA.
DR RefSeq; WP_000273761.1; NC_020376.1.
DR AlphaFoldDB; M1Q576; -.
DR SMR; M1Q576; -.
DR GeneID; 67465630; -.
DR KEGG; btht:H175_ch1074; -.
DR PATRIC; fig|1286404.3.peg.1094; -.
DR HOGENOM; CLU_000445_107_27_9; -.
DR Proteomes; UP000011719; Chromosome.
DR GO; GO:0005886; C:plasma 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 CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 13..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..268
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 287..523
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 510..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63700 MW; 90A525D7FAFE5246 CRC64;
MYFLQNLKVK YKLLALISLA VLGMIIMSSV AINSINKIKH DTEVVVDDYQ YSAILLEGML
RTQNSLEYNL LELITASQNE VANKEGIINN IEKDLKKYDS LLKEYDDGFN LSKQEDELFQ
KMKKSLPSYK DTYKKLFEKA KATNEPQMVN EFQKELKPKG IELAGYAVDL ESYVSNLADQ
VFKDSQKMID RSVITFIILV VVTTIVICIV SYIISKLIVA PLQTVSRMME RAKEGDLTVH
GDYTAKDELG VLVSNFNEMI AGLRTNMQEV ENNIQLLFQY ADGVASASEV SSSAAKKITM
DIEEVANGAE SQMQAMEQTA GAMEELTQGM QSIVNTSSSV NELSAQSALD AESGNKLMKQ
MIQQMDTIQN SVHSGVKQVE TMKEQSEEIV KIIDVMQGIT SQINLLALNA AIEAARAGES
GRGFAIVADE VRKLAEQSSD SAKQIENLIT QVMGTTNHTV HMMGKVDNEV QAGTQVVMHT
EKVFGTITEK VQQVSEQIQT VSMSTDEIAA SSEEISASAE DMAQISQRSS DRTDRVKESI
QQQEKSVQEI SVSIEHMHNA AGKLKQIVAQ FTLQK
//
