ID A0A3S0P4T6_9BACI Unreviewed; 529 AA.
AC A0A3S0P4T6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:RUL50495.1};
GN ORFNames=EK386_13995 {ECO:0000313|EMBL:RUL50495.1};
OS Lysinibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=2498145 {ECO:0000313|EMBL:RUL50495.1, ECO:0000313|Proteomes:UP000287910};
RN [1] {ECO:0000313|EMBL:RUL50495.1, ECO:0000313|Proteomes:UP000287910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SYSU K30002 {ECO:0000313|EMBL:RUL50495.1,
RC ECO:0000313|Proteomes:UP000287910};
RA Narsing Rao M.P., Zhang H., Dong Z.-Y., Niu X.-K., Zhang K., Fang B.-Z.,
RA Kang Y.-Q., Xiao M., Li W.-J.;
RT "Lysinibacillus antri sp. nov., isolated from a cave soil.";
RL Submitted (DEC-2018) 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:RUL50495.1}.
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DR EMBL; RYYR01000020; RUL50495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0P4T6; -.
DR Proteomes; UP000287910; 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; 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..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..265
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 270..506
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 529 AA; 57753 MW; 8C516821FF312D89 CRC64;
MAWLKNIKIS NKLMVINILS IIFILITGIF GMININKMST QTTEMYENQL LPIKWLNDIR
AQSRANEALV KEIILTKDEA ERREFISNIS TRAQSIKDDF ALYKETEITP FEEERLDIIA
QEIERIGANR QELYKILETG TSDDAYAYYK ANLVTPLDTL NKTLQEVADY LSDRAEETLV
QMNNEKRTAT IIMISVLIVA IVLALVLTTI ISRAIVNPLK NVVDVMEEAA KGDLTVSTSH
NSKDEIGQMV TSFNNLMEST RSAIEKVVNA ASELSASSQQ ISASAEEIAS GSQQQAQDAS
ASATMMAEMT TVVEDVARNA EEAARLAENT MNEAKQGGVV INDAIQGMTA IRESIYELSN
KSVQIGEIVE VIDDIAEQTN LLALNAAIEA ARAGEAGKGF AVVADEVRKL AERSSKATKE
ISELVNIIQE NTRNSVKSVE DGSAKAEKVD STFNDILQLV NISSIKVTEI AAANEQQTAQ
AEEVQQSVSS IAAVTEEISA GLQETAATAE VLSEMAEGLN QLTGQFKIK
//
