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Database: UniProt
Entry: B8FT68_DESHD
LinkDB: B8FT68_DESHD
Original site: B8FT68_DESHD 
ID   B8FT68_DESHD            Unreviewed;       429 AA.
AC   B8FT68;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ACL22084.1};
GN   OrderedLocusNames=Dhaf_4075 {ECO:0000313|EMBL:ACL22084.1};
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL22084.1, ECO:0000313|Proteomes:UP000007726};
RN   [1] {ECO:0000313|EMBL:ACL22084.1, 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; ACL22084.1; -; Genomic_DNA.
DR   RefSeq; WP_015945003.1; NC_011830.1.
DR   AlphaFoldDB; B8FT68; -.
DR   KEGG; dhd:Dhaf_4075; -.
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   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        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..124
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          143..379
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   429 AA;  46153 MW;  275DC6A7468DAF17 CRC64;
     MSLVMNGSED LKQVSLFKYI GQTLKVVIPS VVVIAAVIQF ILKLPQFEML VVCGGYLIAG
     LGIAVAASFR NYNRFLKPIQ QMEIGILQVA EGELNTQIQV TSAEMAAVTQ AFNAMTKNFR
     EIIHKIRIMA NEWVESIDEL SANSEEIAAK NEEVSQHIAG MSNGMAQQRT VISRAMDSFR
     ALQDTIQIIA ERARSVAQEA GISQGNAEKG LNGLSGIVQA MQDTNTTVDE ASERIKNLDE
     QSQQIVSITA TIASIARQTN LLALNAAIEA ARAGEHGRGF AVVADEIRKL AEGVSVSTDE
     VAEITNGIQE TITATVDAMK VADSKVENSL QQTLAARQAL EIIVKSTKQV SSDISEIAAS
     GEQILTHMEG VTNQSQQVEY IAAEAEVSTR EIEQASAEVA ASMQNIAEAA QSLVSMAIEL
     REQVAGFKV
//
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