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Database: UniProt
Entry: Q65JL6_BACLD
LinkDB: Q65JL6_BACLD
Original site: Q65JL6_BACLD 
ID   Q65JL6_BACLD            Unreviewed;       377 AA.
AC   Q65JL6; Q62V21;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Flagellar motor switch protein FliN {ECO:0000256|RuleBase:RU362074};
GN   Name=fliY {ECO:0000313|EMBL:AAU23388.1};
GN   OrderedLocusNames=BL01261 {ECO:0000313|EMBL:AAU23388.1};
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU23388.1, ECO:0000313|Proteomes:UP000000606};
RN   [1] {ECO:0000313|EMBL:AAU23388.1, ECO:0000313|Proteomes:UP000000606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC   9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC   {ECO:0000313|Proteomes:UP000000606};
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
CC   -!- FUNCTION: FliN is one of three proteins (FliG, FliN, FliM) that form
CC       the rotor-mounted switch complex (C ring), located at the base of the
CC       basal body. This complex interacts with the CheY and CheZ chemotaxis
CC       proteins, in addition to contacting components of the motor that
CC       determine the direction of flagellar rotation.
CC       {ECO:0000256|RuleBase:RU362074}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362074};
CC       Peripheral membrane protein {ECO:0000256|RuleBase:RU362074};
CC       Cytoplasmic side {ECO:0000256|RuleBase:RU362074}. Bacterial flagellum
CC       basal body {ECO:0000256|RuleBase:RU362074}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the FliN/MopA/SpaO family.
CC       {ECO:0000256|ARBA:ARBA00009226, ECO:0000256|RuleBase:RU362074}.
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DR   EMBL; CP000002; AAU23388.1; -; Genomic_DNA.
DR   RefSeq; WP_003181794.1; NC_006322.1.
DR   AlphaFoldDB; Q65JL6; -.
DR   STRING; 279010.BL01261; -.
DR   GeneID; 66216136; -.
DR   KEGG; bli:BL01261; -.
DR   PATRIC; fig|279010.13.peg.1852; -.
DR   eggNOG; COG1776; Bacteria.
DR   eggNOG; COG1886; Bacteria.
DR   HOGENOM; CLU_033893_0_0_9; -.
DR   Proteomes; UP000000606; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-UniRule.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   CDD; cd17907; FliY_FliN-Y; 1.
DR   Gene3D; 3.40.1550.10; CheC-like; 1.
DR   Gene3D; 2.30.330.10; SpoA-like; 1.
DR   InterPro; IPR007597; CheC.
DR   InterPro; IPR028976; CheC-like_sf.
DR   InterPro; IPR012826; FliN.
DR   InterPro; IPR001543; FliN-like_C.
DR   InterPro; IPR001172; FliN_T3SS_HrcQb.
DR   InterPro; IPR036429; SpoA-like_sf.
DR   NCBIfam; TIGR02480; fliN; 1.
DR   PANTHER; PTHR43484; -; 1.
DR   PANTHER; PTHR43484:SF1; FLAGELLAR MOTOR SWITCH PROTEIN FLIN; 1.
DR   Pfam; PF04509; CheC; 2.
DR   Pfam; PF01052; FliMN_C; 1.
DR   PRINTS; PR00956; FLGMOTORFLIN.
DR   SUPFAM; SSF103039; CheC-like; 1.
DR   SUPFAM; SSF101801; Surface presentation of antigens (SPOA); 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|RuleBase:RU362074};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU362074};
KW   Cell projection {ECO:0000313|EMBL:AAU23388.1};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU362074};
KW   Cilium {ECO:0000313|EMBL:AAU23388.1};
KW   Flagellar rotation {ECO:0000256|ARBA:ARBA00022779,
KW   ECO:0000256|RuleBase:RU362074}; Flagellum {ECO:0000313|EMBL:AAU23388.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000606}.
FT   DOMAIN          34..70
FT                   /note="CheC-like protein"
FT                   /evidence="ECO:0000259|Pfam:PF04509"
FT   DOMAIN          131..166
FT                   /note="CheC-like protein"
FT                   /evidence="ECO:0000259|Pfam:PF04509"
FT   DOMAIN          297..367
FT                   /note="Flagellar motor switch protein FliN-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01052"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   377 AA;  40819 MW;  E120C4286F067F55 CRC64;
     MENNNRLSQD EIDALLKGGD DTAQEQPESG LSLMEQDTIG EIGNISFGSS ATALSTLLNQ
     KVEITTPTVS VIEKSHLNDE FPHPYVSIGV SYTEGFSGNN LLVIKQEDAA IIADLMMGGD
     GTNADPSLGE IHLSAVQEAM NQMMGSAATS MSTVFSKKID ISPPEVDLLD VKEGEGTEQI
     PKEDPLVKVS FRLKVGDLID SHIMQLYPLT FAKDLIDELT NQDGGEEPVK TEEVQTPVQE
     KPAPNPNSAP AQTQRQEPAP KRQGTAKVSE PVQVAPAEFQ SFAPQTEAQP HLQNLDMLMD
     IPLSVTVELG RTNRSVKEVL ELSTGSIIEL DKLAGEPVDI LVNQRVVAKG EVVVIDENFG
     VRVTDILSQA ERISKLR
//
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