ID K0NBL9_DESTT Unreviewed; 174 AA.
AC K0NBL9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Flagellar protein FliL {ECO:0000256|RuleBase:RU364125};
GN Name=fliL {ECO:0000313|EMBL:CCK81734.1};
GN OrderedLocusNames=TOL2_C35770 {ECO:0000313|EMBL:CCK81734.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK81734.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK81734.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
CC -!- FUNCTION: Controls the rotational direction of flagella during
CC chemotaxis. {ECO:0000256|ARBA:ARBA00002254,
CC ECO:0000256|RuleBase:RU364125}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU364125}.
CC Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the FliL family. {ECO:0000256|ARBA:ARBA00008281,
CC ECO:0000256|RuleBase:RU364125}.
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DR EMBL; FO203503; CCK81734.1; -; Genomic_DNA.
DR AlphaFoldDB; K0NBL9; -.
DR STRING; 651182.TOL2_C35770; -.
DR KEGG; dto:TOL2_C35770; -.
DR PATRIC; fig|651182.5.peg.4201; -.
DR HOGENOM; CLU_099018_4_1_7; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR InterPro; IPR005503; FliL.
DR PANTHER; PTHR35091; FLAGELLAR PROTEIN FLIL; 1.
DR PANTHER; PTHR35091:SF2; FLAGELLAR PROTEIN FLIL; 1.
DR Pfam; PF03748; FliL; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU364125};
KW Cell projection {ECO:0000313|EMBL:CCK81734.1};
KW Chemotaxis {ECO:0000256|RuleBase:RU364125};
KW Cilium {ECO:0000313|EMBL:CCK81734.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU364125};
KW Flagellum {ECO:0000313|EMBL:CCK81734.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364125};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364125};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364125}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364125"
SQ SEQUENCE 174 AA; 20305 MW; 506A431AF0F1C468 CRC64;
MKKTSFKKRF KRIFGYKKTI LIIAGFLFFL IIVITGILLF FLKGSAKDTK DVQNSMTSSK
DSLPEVAWEN NVVFEDIVDL EPFERIQLKA NSAMGLISMH LSLELTDPQY KNQVYTMQDR
IRKIITGQVE DMNWLSLRNP EGKIMLKYDL LKRINSIFPK PAVSNIYFTY FIMQ
//
