ID M6JKH8_9LEPT Unreviewed; 174 AA.
AC M6JKH8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Flagellar protein FliL {ECO:0000256|RuleBase:RU364125};
GN Name=fliL {ECO:0000313|EMBL:EMN20050.1};
GN ORFNames=LEP1GSC063_2219 {ECO:0000313|EMBL:EMN20050.1};
OS Leptospira santarosai serovar Arenal str. MAVJ 401.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049976 {ECO:0000313|EMBL:EMN20050.1, ECO:0000313|Proteomes:UP000012106};
RN [1] {ECO:0000313|EMBL:EMN20050.1, ECO:0000313|Proteomes:UP000012106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAVJ 401 {ECO:0000313|EMBL:EMN20050.1,
RC ECO:0000313|Proteomes:UP000012106};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMN20050.1}.
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DR EMBL; AHMU02000077; EMN20050.1; -; Genomic_DNA.
DR RefSeq; WP_004460753.1; NZ_AHMU02000077.1.
DR AlphaFoldDB; M6JKH8; -.
DR GeneID; 29739116; -.
DR Proteomes; UP000012106; Unassembled WGS sequence.
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:EMN20050.1};
KW Chemotaxis {ECO:0000256|RuleBase:RU364125};
KW Cilium {ECO:0000313|EMBL:EMN20050.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU364125};
KW Flagellum {ECO:0000313|EMBL:EMN20050.1};
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 28..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364125"
SQ SEQUENCE 174 AA; 19245 MW; B90A38DA3129E550 CRC64;
MGDAEIDEEE GGLPAAEGGG GASPIIKWLL YVAGAIFGII IVAIVAMVVA RKTAMTTFDQ
RKNVALVKPP PPLANYNFTE EFRINTSDKG EAHFVKMKLA FGIAKEDQTL SAELAERNAQ
MRDLINLIVG RKSKDELINI EDQLDLREEI KAQVNHILTE GKIQEVYFTE FIIN
//
