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Database: UniProt
Entry: B8FVG5_DESHD
LinkDB: B8FVG5_DESHD
Original site: B8FVG5_DESHD 
ID   B8FVG5_DESHD            Unreviewed;       445 AA.
AC   B8FVG5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ACL22367.1};
GN   OrderedLocusNames=Dhaf_4362 {ECO:0000313|EMBL:ACL22367.1};
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL22367.1, ECO:0000313|Proteomes:UP000007726};
RN   [1] {ECO:0000313|EMBL:ACL22367.1, ECO:0000313|Proteomes:UP000007726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP001336; ACL22367.1; -; Genomic_DNA.
DR   RefSeq; WP_011460908.1; NC_011830.1.
DR   AlphaFoldDB; B8FVG5; -.
DR   KEGG; dhd:Dhaf_4362; -.
DR   HOGENOM; CLU_000445_107_18_9; -.
DR   Proteomes; UP000007726; Chromosome.
DR   GO; GO:0016020; C: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   Membrane {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        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          86..139
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          158..408
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   445 AA;  47889 MW;  C14F4973F75D06EE CRC64;
     MNSFLDRISE FFFKHSGIVR WWFNLSVSAK LSLAFGINAL ITLVAGGAVY FMVKTGANLE
     QNILIYLVSL VIAGLIIFIY GLYISYLVAT PLRRGVQFAE KMAQGDLTAT LYSMGQKDEL
     GTLCKSLNQM TENFRSLVGD ITHSADIFAE SSQVLSAQSG GTSESAQLVS SSIHQVASGS
     QTQANSVQNI MSSIQSMAHG IRQIEDHINL ADHSSRQSLQ LAQDGDTAMT MVSLQMGHIH
     NSVDNTGQII TALGEKSTVI GSIVETIKAI SDQTNLLALN AAIEAARAGE HGRGFSVVAE
     EVRKLAEQST LSSAQIETII HDIKTSLDEA ITSMDSEKEV VQSGANAIQN AQQAFTRIKE
     STQVLSEQIQ EISALSSGIT QSADIIAHEV TQVAAICQET TAQTEEVASS SSEQMVAMQE
     INASAQELSK TAQELQYAAR KFILN
//
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