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Database: UniProt/TrEMBL
Entry: B5F933_SALA4
LinkDB: B5F933_SALA4
Original site: B5F933_SALA4 
ID   B5F933_SALA4            Unreviewed;       138 AA.
AC   B5F933;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   29-OCT-2014, entry version 37.
DE   RecName: Full=Flagellar basal body rod protein FlgB {ECO:0000256|PIRNR:PIRNR002889};
GN   Name=flgB {ECO:0000313|EMBL:ACH51145.1};
GN   OrderedLocusNames=SeAg_B2014 {ECO:0000313|EMBL:ACH51145.1};
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH51145.1, ECO:0000313|Proteomes:UP000008819};
RN   [1] {ECO:0000313|EMBL:ACH51145.1, ECO:0000313|Proteomes:UP000008819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483 {ECO:0000313|EMBL:ACH51145.1,
RC   ECO:0000313|Proteomes:UP000008819};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Structural component of flagellum, the bacterial
CC       motility apparatus. Part of the rod structure of flagellar basal
CC       body. {ECO:0000256|PIRNR:PIRNR002889}.
CC   -!- SUBUNIT: The basal body constitutes a major portion of the
CC       flagellar organelle and consists of a number of rings mounted on a
CC       central rod. {ECO:0000256|PIRNR:PIRNR002889}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000256|PIRNR:PIRNR002889}.
CC   -!- SIMILARITY: Belongs to the flagella basal body rod proteins
CC       family. {ECO:0000256|PIRNR:PIRNR002889}.
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DR   EMBL; CP001138; ACH51145.1; -; Genomic_DNA.
DR   RefSeq; YP_002146869.1; NC_011149.1.
DR   STRING; 454166.SeAg_B2014; -.
DR   PRIDE; B5F933; -.
DR   EnsemblBacteria; ACH51145; ACH51145; SeAg_B2014.
DR   PATRIC; 18482322; VBISalEnt65316_1973.
DR   eggNOG; COG1815; -.
DR   HOGENOM; HOG000257191; -.
DR   OMA; LQIEQAN; -.
DR   OrthoDB; EOG6Q8J3B; -.
DR   BioCyc; SENT454166:GHBA-2000-MONOMER; -.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   InterPro; IPR001444; Flag_bb_rod_N.
DR   InterPro; IPR019776; Flagellar_basal_body_rod_CS.
DR   InterPro; IPR006300; FlgB.
DR   Pfam; PF00460; Flg_bb_rod; 1.
DR   PIRSF; PIRSF002889; Rod_FlgB; 1.
DR   TIGRFAMs; TIGR01396; FlgB; 1.
DR   PROSITE; PS00588; FLAGELLA_BB_ROD; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|PIRNR:PIRNR002889};
KW   Cell projection {ECO:0000313|EMBL:ACH51145.1};
KW   Cilium {ECO:0000313|EMBL:ACH51145.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008819};
KW   Flagellum {ECO:0000313|EMBL:ACH51145.1}.
SQ   SEQUENCE   138 AA;  15129 MW;  5964A5B727BE3770 CRC64;
     MLDRLDAALR FQQEALNLRA QRQEILAANI ANADTPGYQA RDIDFASELK KVMVRGREET
     GGVALTLTSS HHIPAQAVSS PAVDLLYRVP DQPSLDGNTV DMDRERTQFA DNSLKYQMGL
     TVLGSQLKGM MNVLQGGN
//
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