ID A0A1V2A8T3_9BACI Unreviewed; 561 AA.
AC A0A1V2A8T3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BTO28_07415 {ECO:0000313|EMBL:OMP67340.1};
OS Domibacillus epiphyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714355 {ECO:0000313|EMBL:OMP67340.1, ECO:0000313|Proteomes:UP000188613};
RN [1] {ECO:0000313|EMBL:OMP67340.1, ECO:0000313|Proteomes:UP000188613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAB 38 {ECO:0000313|EMBL:OMP67340.1,
RC ECO:0000313|Proteomes:UP000188613};
RA Verma A., Ojha A.K., Krishnamurthi S.;
RT "Domibacillus sp. SAB 38T whole genome sequencing.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMP67340.1}.
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DR EMBL; MSFI01000010; OMP67340.1; -; Genomic_DNA.
DR RefSeq; WP_076764909.1; NZ_MSFI01000010.1.
DR AlphaFoldDB; A0A1V2A8T3; -.
DR STRING; 1714355.BTO28_07415; -.
DR OrthoDB; 107771at2; -.
DR Proteomes; UP000188613; Unassembled WGS sequence.
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; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
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; PF05227; CHASE3; 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 Reference proteome {ECO:0000313|Proteomes:UP000188613};
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 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..256
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 275..511
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 561 AA; 60344 MW; 44D878DCC24C8FAB CRC64;
MSIGKKLFSG FLGVIILLCL ITGISVYQLT SITSTYSDLI NLQTAKVINA KEIKYVAAEQ
AKSIRGYVIT GNDKLLQDFE NAQKDFSSAH KKLGTLLETD SGKKMLEELD QLQVDYIQTA
DQVIAYKQQN NTAGYTKLLT GELAPLTDEI SKKAIELEKL CQDVLDQENE TTLQLATQVK
NVLLVVAAIA VLAGFLIAFY IGRIISKPVT KVAQAAKQIA DGNLSISDIE VKNKDEIGEM
AKAFNRMKKD LQELIRKLGE SADQIAASSQ QLSASSEQSM QAASQVTETV QDISTAAEDQ
INSMEDNKKG MEESSAGLQR IAESASTVSE SSTEVLGEAE QGNEIIEKTI HQMEGITVSV
QDVSAVIKDL GENSKEIGNI TAVIKQIADQ TNLLALNAAI EAARAGEHGK GFAVVADEVR
KLAEQSQQSS KQIESIINTI QENTGHAVNV MEKGTEDVKS GTEIVNQAGQ AFRRILNSIQ
EVTTQVQEVS AATEEISAST EQLTGSMDQL TKASAKIATS TQGVAASSEE QLASTQEIAA
SADSLSKLAQ ELQKEVSKFK I
//
