ID A0A1S2LND7_9BACI Unreviewed; 562 AA.
AC A0A1S2LND7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BKP35_10245 {ECO:0000313|EMBL:OIJ12935.1};
OS Anaerobacillus arseniciselenatis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=85682 {ECO:0000313|EMBL:OIJ12935.1, ECO:0000313|Proteomes:UP000180098};
RN [1] {ECO:0000313|EMBL:OIJ12935.1, ECO:0000313|Proteomes:UP000180098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15340 {ECO:0000313|EMBL:OIJ12935.1,
RC ECO:0000313|Proteomes:UP000180098};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-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:OIJ12935.1}.
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DR EMBL; MLQQ01000018; OIJ12935.1; -; Genomic_DNA.
DR RefSeq; WP_071313242.1; NZ_MLQQ01000018.1.
DR AlphaFoldDB; A0A1S2LND7; -.
DR OrthoDB; 107771at2; -.
DR Proteomes; UP000180098; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000180098};
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 177..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 204..257
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 276..512
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 103..130
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 562 AA; 61542 MW; 0DE8F5811365FBCA CRC64;
MKLTVAKKLS FSFFALILFI AGIAGFSYYE TNNVNSLYEE LLDDRVLKED LVQQMIIEIK
DQQVTVRSYL LDSDEYYIDQ FQLAVNNYNE LSNHLEGIVD ETGANYLAQL NQLQEQYEVI
ANEAILMKQE ERTDDMISLL QNEGSPIIIK FAETSNQFLQ YQQMMKDDFR ELVNSSMVTL
ISTLLIVSTI ALLFAAAVTY IISKQISKPV LAIANGAEKI ANGDLTGETL QIKNRDELGR
LAESFNKMHD NLKNMIFKVS DSANDLSASS EQLSASAEQT SSATNQIALS ITNVSENLQN
QSDHVDETNQ TVGQMAVGIQ QITNNVVAVT ESATDVQQLS DEGSAKIKDG IKQMGLVNNK
VSHSKKMVEE LGVQSKEISQ IVDLINNIAD QTNLLALNAA IESARAGEAG RGFAVVADEV
RKLAEKSTKS TKQISTIVEQ IQLKIAAIVE AMDSGAHEVN KGVTAVNQTG EAFKKIQKAV
NNTAGQMQDV SAAAQQLASG SDEVTKAMND VRKLNHSITG QSQEVSVAAE EQLSSMEEVS
HSANQLADMA EELQELVMSF KV
//
