ID A3YAV1_9GAMM Unreviewed; 134 AA.
AC A3YAV1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 03-MAY-2023, entry version 44.
DE RecName: Full=Flagellar protein FliL {ECO:0000256|RuleBase:RU364125};
GN ORFNames=MED121_09098 {ECO:0000313|EMBL:EAQ65710.1};
OS Marinomonas sp. MED121.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ65710.1, ECO:0000313|Proteomes:UP000003436};
RN [1] {ECO:0000313|EMBL:EAQ65710.1, ECO:0000313|Proteomes:UP000003436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED121 {ECO:0000313|EMBL:EAQ65710.1,
RC ECO:0000313|Proteomes:UP000003436};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) 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 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}.
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:EAQ65710.1}.
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DR EMBL; AANE01000005; EAQ65710.1; -; Genomic_DNA.
DR RefSeq; WP_009834124.1; NZ_CH672431.1.
DR AlphaFoldDB; A3YAV1; -.
DR STRING; 314277.MED121_09098; -.
DR HOGENOM; CLU_099018_10_2_6; -.
DR Proteomes; UP000003436; 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 inner membrane {ECO:0000256|RuleBase:RU364125};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000313|EMBL:EAQ65710.1};
KW Chemotaxis {ECO:0000256|RuleBase:RU364125};
KW Cilium {ECO:0000313|EMBL:EAQ65710.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU364125};
KW Flagellum {ECO:0000313|EMBL:EAQ65710.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364125};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..134
FT /note="Flagellar protein FliL"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002662907"
SQ SEQUENCE 134 AA; 14891 MW; 80A44243DBA3E0DA CRC64;
MLFRLVLSLL FSGFILASSA FAENDSSELP VYIELRPDFI VNYTTDNNRL KYIKASITIR
ATGAQNAGII ESNMPIVRDG LVIYLSELRA EQVTGAIARE ESRKGAAIFL NEKLKEETGI
EPVKDVLFSS FVTQ
//