ID A0A078KM45_9FIRM Unreviewed; 869 AA.
AC A0A078KM45;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0008006|Google:ProtNLM};
GN ORFNames=CCDG5_0454 {ECO:0000313|EMBL:CDZ23592.1};
OS [Clostridium] cellulosi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=29343 {ECO:0000313|EMBL:CDZ23592.1, ECO:0000313|Proteomes:UP000032431};
RN [1] {ECO:0000313|Proteomes:UP000032431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5 {ECO:0000313|Proteomes:UP000032431};
RA Wibberg D.;
RL Submitted (JUL-2014) 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; LM995447; CDZ23592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078KM45; -.
DR STRING; 29343.CCDG5_0454; -.
DR KEGG; ccel:CCDG5_0454; -.
DR PATRIC; fig|29343.3.peg.475; -.
DR HOGENOM; CLU_330025_0_0_9; -.
DR OrthoDB; 1862723at2; -.
DR Proteomes; UP000032431; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.20.120.1530; -; 3.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF18947; HAMP_2; 3.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 3.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000032431};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 388..440
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 580..809
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 824..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 95044 MW; A87B78CA6A221D6E CRC64;
MKKENIRQNK RKIALPLLVA YILAFCAGLF GACAITGPQS SKIIFGVLFF VFFIALLITV
TLTVRKTNNI FKSVKKLLDD GKYYKAVLDC IPFPVHAVDN NMKWKFVNKA FEKSLVKSGK
IADRKSAYGM VCSTAGANIC NNEKCGIKQL QKGVHESYFE WSGNKCRLNA AAIVGENGEK
LGYVETVTNL TKLIENEEYY KKAIANLMSN LEKLSRGDLD LDLSVPEANS NTQESRETFV
MINESLGRVK ESLELLTNDA AYLRAAAVEG RLDTRVDASG HSGVYQKIIS GIDDTLEAIV
KPVKFTTEYI LKLANGEDLE EIENTYSGDY AVLMNSLNSV RESLYTLLDE SIKLLEAGRE
GNLTARADTS KFKGGYAKVI AGINGMFEAF ATPLNEANEI LALMANNDFT RGMDKDYNGE
FGKLAESVNK LRETFLIIEE LLIEISNGDL SQLEEIMKMP KRSENDRLRP AFIEMMKSVK
QLVDEANMLA ESAANGKLSV RGNAAGLKGE YGEVVAHINR MIEAVEKPFN DLVFVLEKWT
EGDLTAEIDK EYIGDYLRIK NAVNTTGEKF RQMLNSINEA ASQVASGSKE IASGSQNLSR
GTTEQASSIE ELTAAISEIA EQTKNNAKNA ENAKSLSLEV QKEAIEGNEK MKSMQEAMRG
ISDSSANIAK IIKVIDDIAF QTNILSLNAA VEAARAGQAG KGFAVVAQEV RTLASRSATA
AKETTQLIED SSKRVEIGAK IVDETAAEFE KIMQSIEKTT KLVGEISEAS AKQATGITQI
DKGIEQVSTV VQTNSATAEE SAAASEQLSA QAQALRDMVS QFKLGKSSEE PVEKSNVKAE
RNAAPAIQEK ETQPKIVLDD KPQGDYGKY
//