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Database: UniProt
Entry: W4EN88_9BACL
LinkDB: W4EN88_9BACL
Original site: W4EN88_9BACL 
ID   W4EN88_9BACL            Unreviewed;       575 AA.
AC   W4EN88;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Chemoreceptor protein A {ECO:0000313|EMBL:ETT81472.1};
GN   ORFNames=C176_18467 {ECO:0000313|EMBL:ETT81472.1};
OS   Viridibacillus arenosi FSL R5-213.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX   NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT81472.1, ECO:0000313|Proteomes:UP000019062};
RN   [1] {ECO:0000313|EMBL:ETT81472.1, ECO:0000313|Proteomes:UP000019062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT81472.1,
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   -!- 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:ETT81472.1}.
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DR   EMBL; ASQA01000037; ETT81472.1; -; Genomic_DNA.
DR   RefSeq; WP_038189364.1; NZ_ASQA01000037.1.
DR   AlphaFoldDB; W4EN88; -.
DR   PATRIC; fig|1227360.4.peg.3755; -.
DR   eggNOG; COG0840; Bacteria.
DR   Proteomes; UP000019062; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
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; cd11386; MCP_signal; 1.
DR   Gene3D; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR025991; Chemoreceptor_zinc-bind_dom.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR044398; Globin-sensor_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; PF13682; CZB; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF11563; Protoglobin; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   4: Predicted;
KW   Receptor {ECO:0000313|EMBL:ETT81472.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019062};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}.
FT   DOMAIN          200..413
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   575 AA;  65277 MW;  35F2E85F4933EAEE CRC64;
     MFATIRPKLE MAQLLQRGTD INTIGRFKDT LAFNNFHKRD EENLKELYSK LLECTPSMRD
     IFTKYLEEIA PEKHNPISDQ YIEKYLNAFF LLPRDEKYVD ETVRFFYLFR HHKFEPGKTI
     VIFNQFAFYV TTHILYNFGY KPAKAFDLMR SFQGAVNIDQ ELLFEVATER MIEHAVSEVS
     ALMDTNSQIM YMKDLVYSLD RQNEEIQSST AATEQITASI SEVAKTSARI SEKTADSVEY
     ATNSKNTIDL ALNEIFKTEE TFTSIVESFS ELQKRVNDIE NVVTLIKEIA DQTNLLALNA
     SIEAARAGEH GKGFAVVAQE VRKLAENTVS ALGEVSSNVQ HLKSYSSNVA TSISQTTTII
     KEATNEAKDS LPLLSSIVEA IEEINVDVTN TAAISEQQAA AIDEVSHRMV QISDLQDDIR
     ELGQATSAGI HQLGAEINHF RLSIVENNNV QLSSNALLQL SKADHILWKW RVYNMFLGLE
     KIEESEVSSH RDCRLGKWYS SEKARDRFGK EKAYIELDAY HQKVHEAAKR AAVSYNAGKI
     SDAELALKEV ESSSQQVLHF INELIEKLEK ERFII
//
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