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Database: UniProt
Entry: A0A1S6ISD8_9FIRM
LinkDB: A0A1S6ISD8_9FIRM
Original site: A0A1S6ISD8_9FIRM 
ID   A0A1S6ISD8_9FIRM        Unreviewed;       640 AA.
AC   A0A1S6ISD8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Methyl-accepting chemotaxis sensory transducer with Cache sensor {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B0537_00215 {ECO:0000313|EMBL:AQS57686.1};
OS   Desulforamulus ferrireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS57686.1, ECO:0000313|Proteomes:UP000189464};
RN   [1] {ECO:0000313|EMBL:AQS57686.1, ECO:0000313|Proteomes:UP000189464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSS09 {ECO:0000313|EMBL:AQS57686.1,
RC   ECO:0000313|Proteomes:UP000189464};
RX   PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA   Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT   "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT   sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT   compost.";
RL   Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP019698; AQS57686.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S6ISD8; -.
DR   STRING; 1833852.B0537_00215; -.
DR   KEGG; dfg:B0537_00215; -.
DR   OrthoDB; 9760371at2; -.
DR   Proteomes; UP000189464; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; 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   CDD; cd12913; PDC1_MCP_like; 1.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 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   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189464};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        302..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          323..377
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          375..625
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   640 AA;  70572 MW;  A0778020AEC96FD1 CRC64;
     MKSIKGLFIG TAITVVIIVF AAQTGLGLYQ FNKIISQDID TILEYQVEKE AAYLNNRIAD
     VGKVSYSLAA NIKAMSTYNT DYMLEMIKPY ITAEEMAIGA GFWFEPYAFN PDQKYYGPYV
     YKENGEIQIT WDYSNEEYDY FKYDWYQDTL KSKQRVVYSE PYLDTVSGML MLTTSSLITK
     DDRILGVTTC DINIDELQNY VRNIKVGEEG YAFIVTGQGY YLAHRDNDKN LNEKITEDQD
     ESIKALGQKI LASNKNELAE VSMTGQEYYV AYAPVGETGL KIVLAMPSHE ISSVINNYMK
     TIIFSSVVSI ILLILVLYWL ITKKITNPLQ MLVKETQRFA DGDLQINQDN PIKTKDEIGL
     LAQAFRDMVV QMNVLVKEIV EKSRQVATAA QQMNASATQT SAGAIETAST MNEISATVEN
     VAANMDDVSN VSKTSAALAQ EGGREIAKVN EQMQEITDST RSVAGVIQGL SQRSQEINQI
     VELITGIADQ TNLLALNAAI EAARAGEQGR GFAVVADEVR RLAEQTAGAT KQINGLIASV
     QTEAQRAETQ INENVTTVQN GSLLVQELGH KFSRIAEDVE GLAQQIAQVV AATEELNSGV
     QNVAAAAEEQ TASMEEVSAT SESLEKLAKE LSSLVEKFKV
//
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