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Database: UniProt
Entry: T0BZN3_ALIAG
LinkDB: T0BZN3_ALIAG
Original site: T0BZN3_ALIAG 
ID   T0BZN3_ALIAG            Unreviewed;       145 AA.
AC   T0BZN3; A0A9E6ZDK2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Flagellar protein FliL {ECO:0000256|RuleBase:RU364125};
GN   ORFNames=K1I37_10120 {ECO:0000313|EMBL:UNO47112.1};
OS   Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS   / NCIMB 13137 / GD3B).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=1356854 {ECO:0000313|EMBL:UNO47112.1, ECO:0000313|Proteomes:UP000829401};
RN   [1] {ECO:0000313|Proteomes:UP000829401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3922 {ECO:0000313|Proteomes:UP000829401};
RX   PubMed=36240455; DOI=10.1093/g3journal/jkac225;
RA   Leonardo I.C., Barreto Crespo M.T., Gaspar F.B.;
RT   "Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris
RT   DSM 3922T, a taint-producing strain.";
RL   G3 (Bethesda) 12:0-0(2022).
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; CP080467; UNO47112.1; -; Genomic_DNA.
DR   RefSeq; WP_021296457.1; NZ_AURB01000129.1.
DR   STRING; 1356854.N007_07100; -.
DR   KEGG; aaco:K1I37_10120; -.
DR   Proteomes; UP000829401; 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:UNO47112.1};
KW   Chemotaxis {ECO:0000256|RuleBase:RU364125};
KW   Cilium {ECO:0000313|EMBL:UNO47112.1};
KW   Flagellar rotation {ECO:0000256|RuleBase:RU364125};
KW   Flagellum {ECO:0000313|EMBL:UNO47112.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000829401};
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        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364125"
SQ   SEQUENCE   145 AA;  16055 MW;  83B79D25E5B81623 CRC64;
     MKSPVRVMLL IIIGILVIAG GGVAVAMYMK HQHHTGTAKA HALSAKEAAA LQVTLPQMTT
     NLESSGLIQF TLTLQADNKS TKKELSLMQY QIQDDVNEIM RQYTPNQLRN DKCLNNLKQV
     IQKDINGMLD TGNVTNVYFS QVLVQ
//
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