ID B8EL20_METSB Unreviewed; 168 AA.
AC B8EL20;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Flagellar protein FliL {ECO:0000256|RuleBase:RU364125};
GN OrderedLocusNames=Msil_0032 {ECO:0000313|EMBL:ACK49015.1};
OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS 13906 / BL2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK49015.1, ECO:0000313|Proteomes:UP000002257};
RN [1] {ECO:0000313|EMBL:ACK49015.1, ECO:0000313|Proteomes:UP000002257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2
RC {ECO:0000313|Proteomes:UP000002257};
RX PubMed=20472789; DOI=10.1128/JB.00506-10;
RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT "Complete genome sequence of the aerobic facultative methanotroph
RT Methylocella silvestris BL2.";
RL J. Bacteriol. 192:3840-3841(2010).
CC -!- FUNCTION: Controls the rotational direction of flagella during
CC chemotaxis. {ECO:0000256|ARBA:ARBA00002254,
CC ECO:0000256|RuleBase:RU364125}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU364125}. Membrane
CC {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; CP001280; ACK49015.1; -; Genomic_DNA.
DR RefSeq; WP_012589085.1; NC_011666.1.
DR AlphaFoldDB; B8EL20; -.
DR STRING; 395965.Msil_0032; -.
DR KEGG; msl:Msil_0032; -.
DR eggNOG; COG1580; Bacteria.
DR HOGENOM; CLU_125894_1_0_5; -.
DR OrthoDB; 7908910at2; -.
DR Proteomes; UP000002257; 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 Pfam; PF03748; FliL; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|RuleBase:RU364125};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000313|EMBL:ACK49015.1};
KW Chemotaxis {ECO:0000256|RuleBase:RU364125};
KW Cilium {ECO:0000313|EMBL:ACK49015.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU364125};
KW Flagellum {ECO:0000313|EMBL:ACK49015.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364125};
KW Reference proteome {ECO:0000313|Proteomes:UP000002257};
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..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364125"
SQ SEQUENCE 168 AA; 17350 MW; 17BFE72C6C47DDA4 CRC64;
MSTDEDYDLE AASTRPAGAS LAAFAGLMAA LTIVAMISGG ALGARLGAVV KTQLAGAPGS
ARADAQSAYS GGVNLQDLPP IIANLAEPSD AWVRLQATLV LDRPASGKPD VLAAQIAEDI
LGFMRTATLS QIAGASGLQH LREDLNERAM IRSDGRVREL ILQTLVVQ
//