ID G2IEE4_9CLOT Unreviewed; 150 AA.
AC G2IEE4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Flagellar protein FliL {ECO:0000256|RuleBase:RU364125};
GN Name=fliL {ECO:0000313|EMBL:BAK81518.1};
GN ORFNames=RATSFB_0956 {ECO:0000313|EMBL:BAK81518.1};
OS Candidatus Arthromitus sp. SFB-rat-Yit.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1041504 {ECO:0000313|EMBL:BAK81518.1, ECO:0000313|Proteomes:UP000001273};
RN [1] {ECO:0000313|EMBL:BAK81518.1, ECO:0000313|Proteomes:UP000001273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-rat-Yit {ECO:0000313|EMBL:BAK81518.1};
RX PubMed=21925114;
RA Prakash T., Oshima K., Morita H., Fukuda S., Imaoka A., Kumar N.,
RA Sharma V.K., Kim S.-W., Takahashi M., Saitou N., Taylor T.D., Ohno H.,
RA Umesaki Y., Hattori M.;
RT "Complete genome sequences of rat and mouse segmented filamentous bacteria,
RT a potent inducer of th17 cell differentiation.";
RL Cell Host Microbe 10:273-284(2011).
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; AP012210; BAK81518.1; -; Genomic_DNA.
DR RefSeq; WP_014094978.1; NC_016012.1.
DR AlphaFoldDB; G2IEE4; -.
DR STRING; 1041504.RATSFB_0956; -.
DR KEGG; asb:RATSFB_0956; -.
DR eggNOG; COG1580; Bacteria.
DR HOGENOM; CLU_099018_6_2_9; -.
DR OrthoDB; 9799777at2; -.
DR Proteomes; UP000001273; 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:BAK81518.1};
KW Chemotaxis {ECO:0000256|RuleBase:RU364125};
KW Cilium {ECO:0000313|EMBL:BAK81518.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU364125};
KW Flagellum {ECO:0000313|EMBL:BAK81518.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364125};
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 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364125"
SQ SEQUENCE 150 AA; 16608 MW; 5CA9305200AE2F61 CRC64;
MASEEKKKSG KGVIIIVIVL LLVIVIGGVA GFFIISKMNN NSDEPKKIVE EVMQLDDIVV
NIKDPSNKKY VKASLAMTYD SKNKKALESI NSNIYKIKDT IITIFKNKSL SEVETSEGIE
AIKLEIKNAV NSILESEVLL SVYFTNLLVN
//
