ID W4ENH5_9BACL Unreviewed; 569 AA.
AC W4ENH5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ETT81562.1};
GN ORFNames=C176_18917 {ECO:0000313|EMBL:ETT81562.1};
OS Viridibacillus arenosi FSL R5-213.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT81562.1, ECO:0000313|Proteomes:UP000019062};
RN [1] {ECO:0000313|EMBL:ETT81562.1, ECO:0000313|Proteomes:UP000019062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT81562.1,
RC ECO:0000313|Proteomes:UP000019062};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT81562.1}.
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DR EMBL; ASQA01000037; ETT81562.1; -; Genomic_DNA.
DR RefSeq; WP_038189657.1; NZ_ASQA01000037.1.
DR AlphaFoldDB; W4ENH5; -.
DR PATRIC; fig|1227360.4.peg.3848; -.
DR eggNOG; COG0840; Bacteria.
DR Proteomes; UP000019062; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 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 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019062};
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 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 283..540
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 148..175
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 569 AA; 62249 MW; 4B663B920DCADD10 CRC64;
MKLGKKLGFK NFKTVRAKIS FGFIIVVLIM TGYNVYSYVM QQNSTKSTKE IVEVELEILA
ADDELASSFA NRTAAARGYI ISGDKKYKEK FDEYTDIAEE NAAIVAGLTS SIKLDEIVEK
ARVWQTYIKE DVFEEYDRGN KQLAADNLKS VDEQASEIQE GYEELANTRE EAIKKIGKEM
IENGENNQLI SIISTILLTI ISVIVAYITA RIIVKPIKLV AKRMTEISQG DISQPDLPKT
SEDEIGQLIE ATNSMSKNVH EILSNIQDVS NQVASNSEEL AQSALEVKTG STQIALTMQE
IAEGTESQAS NASDLATVME SFTQKVKEAN YEGEKMNNHT SNVQSLTHEG SKLMIDSTEQ
MRKIDGIVQE SVRKVENLAV QSLEISKLVS VITSIADQTN LLALNAAIEA ARAGEQGKGF
AVVADEVRKL AEQVTLSVTD IAGIVQKIQQ ETKNVTTSLQ SGYEEVIQGT EQIASTGETF
NNISNAISDM IDNINVISNN LSGISQTTLQ INHSIDDIAA VSQESAAGVE ETTATVQQTT
SSMEEISNSS DHLAELAEEL NLQVQKFKL
//