ID I0AMM9_IGNAJ Unreviewed; 170 AA.
AC I0AMM9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Flagellar protein FliL {ECO:0000256|RuleBase:RU364125};
GN OrderedLocusNames=IALB_2533 {ECO:0000313|EMBL:AFH50236.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH50236.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH50236.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH50236.1; -; Genomic_DNA.
DR AlphaFoldDB; I0AMM9; -.
DR STRING; 945713.IALB_2533; -.
DR KEGG; ial:IALB_2533; -.
DR eggNOG; COG1580; Bacteria.
DR HOGENOM; CLU_099018_2_0_10; -.
DR Proteomes; UP000007394; 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:AFH50236.1};
KW Chemotaxis {ECO:0000256|RuleBase:RU364125};
KW Cilium {ECO:0000313|EMBL:AFH50236.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU364125};
KW Flagellum {ECO:0000313|EMBL:AFH50236.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364125};
KW Reference proteome {ECO:0000313|Proteomes:UP000007394};
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 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364125"
FT REGION 34..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 170 AA; 18903 MW; EE294393DD0B3BD0 CRC64;
MKPKLLIVGL PLFIVQLVVV YFITANILIP KDHNSGNKEE VKQEQSSDEK KENKSNDDEK
SSEQEGNTSL GENIFNLDDI IVNPAETNGK TLVLASLGFD LNTAEAKKTM EEKVIIVKDA
VITLLSSKTV PQLSNTAYRD SLKSEMISDL SKKMPGVKIN NIYFSKFIIQ
//
