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Database: UniProt
Entry: A0A292YNV9_9BACL
LinkDB: A0A292YNV9_9BACL
Original site: A0A292YNV9_9BACL 
ID   A0A292YNV9_9BACL        Unreviewed;       570 AA.
AC   A0A292YNV9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:GAX90453.1};
GN   ORFNames=EFBL_2080 {ECO:0000313|EMBL:GAX90453.1};
OS   Effusibacillus lacus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Effusibacillus.
OX   NCBI_TaxID=1348429 {ECO:0000313|EMBL:GAX90453.1, ECO:0000313|Proteomes:UP000217785};
RN   [1] {ECO:0000313|Proteomes:UP000217785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=skLN1 {ECO:0000313|Proteomes:UP000217785};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Draft genome sequence of Effusibacillus lacus strain skLN1.";
RL   Submitted (JUL-2017) 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:GAX90453.1}.
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DR   EMBL; BDUF01000057; GAX90453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A292YNV9; -.
DR   Proteomes; UP000217785; 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; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 3.
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:UP000217785};
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        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          212..265
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          284..520
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   570 AA;  62218 MW;  54F83F576E66BFAF CRC64;
     MIKKFKDLRL TVKITSLAVA LVLTSVIAIV VAGYNVNFKQ VMEAAGEELY GCASITSGLF
     TPVDIEDMLA GKQPTPSVQS KIDWIIDHKP IFMNAAIMTL DGKLLAPDKN LIKEGFKSGD
     KFHIDQEAVN MMKTMKHPTY SGIYTFGQHE RQTGYAPIYK DHDPSKEIIA MMAIDFDSDI
     IYSRTWDSLR LIIVISVIFP IFTGFTIYLV VRRMLKPIQS VGEYAKRVAE GDLTIGELTV
     ANRDEVGLLT EDFNKMAGSL KNIIQLVALN AHQVAASSEQ LTASAEHTSR ATGQITQAIQ
     QIAAGTDQQL TRVHRTNDAV GEISSGIQQI AEGVQTVAHS SLKASETAED GNRAMRHMME
     QMSQINQKVQ RTSVIIETLN EKSAEIGQMV TLITDIARQT NLLALNAAIE AARAGEQGKG
     FSVVADEVRK LAEQSGTAAE QIRQNIQVVQ SEIENAVTSM HDGTLAAQEG LSIVAQTGES
     FRHIVAAVEE VSSQVQDINQ NVKRIHDGTQ SLVESIEEIS DLSQQFAGNA QNVAAAAEEQ
     NTTVEEIASS SAMLTRMAAE LQEAVNRFRL
//
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