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Database: UniProt
Entry: B9NT80_9RHOB
LinkDB: B9NT80_9RHOB
Original site: B9NT80_9RHOB 
ID   B9NT80_9RHOB            Unreviewed;       176 AA.
AC   B9NT80;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Flagellar protein FliL {ECO:0000256|RuleBase:RU364125};
GN   Name=fliL {ECO:0000313|EMBL:EEE37314.1};
GN   ORFNames=RKLH11_1150 {ECO:0000313|EMBL:EEE37314.1};
OS   Rhodobacteraceae bacterium KLH11.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE37314.1, ECO:0000313|Proteomes:UP000005135};
RN   [1] {ECO:0000313|Proteomes:UP000005135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX   PubMed=21742885; DOI=10.1128/jb.05556-11;
RA   Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT   "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT   Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL   J. Bacteriol. 193:5011-5012(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; DS999531; EEE37314.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9NT80; -.
DR   STRING; 467661.RKLH11_1150; -.
DR   eggNOG; COG1580; Bacteria.
DR   HOGENOM; CLU_099018_2_1_5; -.
DR   Proteomes; UP000005135; 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   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:EEE37314.1};
KW   Chemotaxis {ECO:0000256|RuleBase:RU364125};
KW   Cilium {ECO:0000313|EMBL:EEE37314.1};
KW   Flagellar rotation {ECO:0000256|RuleBase:RU364125};
KW   Flagellum {ECO:0000313|EMBL:EEE37314.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005135};
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        31..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364125"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   176 AA;  19022 MW;  60B0AD5849DBDB27 CRC64;
     MTVAERMDED PMTDATADEA EATKKSGKKG LVLGLFLALV GGVGGYFITA SGLLPFANQE
     VAKDADKKGE GASVKGLPDV AFVDLPPVII SVNTSDSRHL KFHAQLEVNA GYTADIEKMQ
     PRIMDVLNSY LRAVELTDLE DSLALVRIRG HLLRRIGIVV GEGRVRDVLV MEFVLN
//
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