ID D3RVY7_ALLVD Unreviewed; 140 AA.
AC D3RVY7;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Flagellar protein FliL {ECO:0000256|RuleBase:RU364125};
GN OrderedLocusNames=Alvin_2231 {ECO:0000313|EMBL:ADC63150.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC63150.1, ECO:0000313|Proteomes:UP000001441};
RN [1] {ECO:0000313|EMBL:ADC63150.1, ECO:0000313|Proteomes:UP000001441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC {ECO:0000313|Proteomes:UP000001441};
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(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 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; CP001896; ADC63150.1; -; Genomic_DNA.
DR RefSeq; WP_012971422.1; NC_013851.1.
DR AlphaFoldDB; D3RVY7; -.
DR STRING; 572477.Alvin_2231; -.
DR KEGG; alv:Alvin_2231; -.
DR eggNOG; COG1580; Bacteria.
DR HOGENOM; CLU_099018_10_3_6; -.
DR OrthoDB; 5616092at2; -.
DR Proteomes; UP000001441; 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 inner membrane {ECO:0000256|RuleBase:RU364125};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000313|EMBL:ADC63150.1};
KW Chemotaxis {ECO:0000256|RuleBase:RU364125};
KW Cilium {ECO:0000313|EMBL:ADC63150.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU364125};
KW Flagellum {ECO:0000313|EMBL:ADC63150.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364125};
KW Reference proteome {ECO:0000313|Proteomes:UP000001441};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..140
FT /note="Flagellar protein FliL"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003050233"
SQ SEQUENCE 140 AA; 15661 MW; 490204BF1DE377C8 CRC64;
MTSVQRKTAY LLALLLGLAP LTSLTAQASE EEAAASPYPG YMALEPPLIV NLAKPRSYLK
LSLQFFIETQ TDADLITLHM PRLRDRMISL LGGRDGEQIM TTEAREQLRI ELLDSLRKTM
MEQTGRPAIS AVYFTDFIAQ
//
