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Database: UniProt
Entry: A4J3Q7_DESRM
LinkDB: A4J3Q7_DESRM
Original site: A4J3Q7_DESRM 
ID   A4J3Q7_DESRM            Unreviewed;       283 AA.
AC   A4J3Q7;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ABO49710.1};
GN   OrderedLocusNames=Dred_1176 {ECO:0000313|EMBL:ABO49710.1};
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO49710.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO49710.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO49710.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000612; ABO49710.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4J3Q7; -.
DR   STRING; 349161.Dred_1176; -.
DR   KEGG; drm:Dred_1176; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_085649_0_0_9; -.
DR   OMA; MMIIVEA; -.
DR   OrthoDB; 3192at2; -.
DR   Proteomes; UP000001556; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}.
FT   DOMAIN          109..283
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   283 AA;  30107 MW;  64574C7698637AA5 CRC64;
     MIKVGIVGGG QGGSAMLRLM SSLTDITVIG IADINENAPA FTVAKELGIP TFLDFKQLLQ
     SANLDVVLDV TGNASVNQAI LEHKQATTHL ADPVISKLMY TVARGQEESA QELKGQAQQL
     ASMAEELNST VHSVPSAIKS VTGALETHCE KLNSAVFQAE KHINDTDEVI EFIKKVADQT
     KLLGLNAAIE AARAGNHGRG FGVVANEVRK LAEDSVVSAK KISNILGNIE DSMKTIILGI
     DETATIAQMQ QSTTDKVDEA TKQLGQIADE MKVFAHKLSN FAS
//
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