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Database: UniProt/TrEMBL
Entry: E8VAJ7_BACST
LinkDB: E8VAJ7_BACST
Original site: E8VAJ7_BACST 
ID   E8VAJ7_BACST            Unreviewed;       338 AA.
AC   E8VAJ7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   01-MAY-2013, entry version 17.
DE   RecName: Full=Flagellar motor switch protein FliG;
GN   Name=fliG; OrderedLocusNames=BSn5_20220;
OS   Bacillus subtilis (strain BSn5).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=936156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSn5;
RX   PubMed=21317323; DOI=10.1128/JB.00129-11;
RA   Deng Y., Zhu Y., Wang P., Zhu L., Zheng J., Li R., Ruan L., Peng D.,
RA   Sun M.;
RT   "Complete genome sequence of Bacillus subtilis BSn5, an endophytic
RT   bacterium of Amorphophallus konjac with antimicrobial activity to
RT   plant pathogen Erwinia carotovora subsp. carotovora.";
RL   J. Bacteriol. 193:2070-2071(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BSn5;
RA   Deng Y., Sun M.;
RT   "Complete Genome Sequence of Bacillus Subtilis BSn5, a Strain of
RT   Plant-associated Bacterium with Antimicrobial Activity to Soil-borne
RT   Plant Pathogens.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the proteins that forms a switch complex that is
CC       proposed to be located at the base of the basal body. This complex
CC       interacts with chemotaxis proteins (such as CheY) in addition to
CC       contacting components of the motor that determine the direction of
CC       flagellar rotation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the FliG family.
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DR   EMBL; CP002468; ADV96648.1; -; Genomic_DNA.
DR   RefSeq; YP_004207675.1; NC_014976.1.
DR   ProteinModelPortal; E8VAJ7; -.
DR   SMR; E8VAJ7; 6-338.
DR   EnsemblBacteria; ADV96648; ADV96648; BSn5_20220.
DR   GeneID; 10184772; -.
DR   KEGG; bsn:BSn5_20220; -.
DR   PATRIC; 46875580; VBIBacSub180317_4124.
DR   HOGENOM; HOG000257646; -.
DR   KO; K02410; -.
DR   BioCyc; BSUB936156:GHCY-4125-MONOMER; -.
DR   GO; GO:0009288; C:bacterial-type flagellum; IEA:InterPro.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0001539; P:ciliary or flagellar motility; IEA:InterPro.
DR   InterPro; IPR000090; Flg_Motor_Flig.
DR   InterPro; IPR011002; FliG_a-hlx.
DR   PIRSF; PIRSF003161; FliG; 1.
DR   PRINTS; PR00954; FLGMOTORFLIG.
DR   SUPFAM; SSF48029; FliG_like; 2.
DR   TIGRFAMs; TIGR00207; fliG; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell membrane; Chemotaxis; Complete proteome;
KW   Flagellar rotation; Flagellum; Membrane.
SQ   SEQUENCE   338 AA;  38191 MW;  8C44193BA0ADE58E CRC64;
     MARRDQDKLT GKQKAAILMI SLGLDVSASV YKHLTDEEIE RLTLEISGVR SVDHQKKDEI
     IEEFHNIAIA QDYISQGGLS YARQVLEKAL GEDKAENILN RLTSSLQVKP FDFARKAEPE
     QILNFIQQEH PQTMALILSY LDPVQAGQIL SELNPEVQAE VARRIAVMDR TSPEIINEVE
     RILEQKLSSA FTQDYTQTGG IEAVVEVLNG VDRGTEKTIL DSLEIQDPDL AEEIKKRMFV
     FEDIVTLDNR AIQRVIRDVE NDDLLLSLKV ASEEVKEIVF NNMSQRMVET FKEEMEFMGP
     VRLKDVEEAQ SRIVSIVRKL EEAGEIVIAR GGGDDIIV
//
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