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FLIL_CAUVN
ID   FLIL_CAUVN              Reviewed;         205 AA.
AC   B8GXB6; P34008;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Flagellar FliL protein;
GN   Name=fliL; OrderedLocusNames=CCNA_02141;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1315735; DOI=10.1128/jb.174.10.3327-3338.1992;
RA   Yu J., Shapiro L.;
RT   "Early Caulobacter crescentus genes fliL and fliM are required for
RT   flagellar gene expression and normal cell division.";
RL   J. Bacteriol. 174:3327-3338(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=7932752; DOI=10.1006/jmbi.1994.1650;
RA   Jenal U., White J., Shapiro L.;
RT   "Caulobacter flagellar function, but not assembly, requires FliL, a non-
RT   polarly localized membrane protein present in all cell types.";
RL   J. Mol. Biol. 243:227-244(1994).
RN   [4]
RP   ERRATUM OF PUBMED:7932752.
RA   Jenal U., White J., Shapiro L.;
RL   J. Mol. Biol. 248:883-883(1995).
CC   -!- FUNCTION: Controls the rotational direction of flagella during
CC       chemotaxis. {ECO:0000269|PubMed:7932752}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:7932752};
CC       Single-pass membrane protein {ECO:0000269|PubMed:7932752}.
CC       Note=Distributed throughout the cell inner membrane and not just at the
CC       poles;.
CC   -!- INDUCTION: Found in all cell types and all developmental stages (at
CC       protein level), the transcript is turned off in swarmer cells and
CC       turned on in stalked cells. {ECO:0000269|PubMed:7932752}.
CC   -!- DISRUPTION PHENOTYPE: Forms a complete but paralyzed flagellum.
CC       {ECO:0000269|PubMed:7932752}.
CC   -!- SIMILARITY: Belongs to the FliL family. {ECO:0000305}.
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DR   EMBL; M85232; AAA62448.1; -; Genomic_DNA.
DR   EMBL; CP001340; ACL95606.1; -; Genomic_DNA.
DR   RefSeq; WP_012640398.1; NC_011916.1.
DR   RefSeq; YP_002517514.1; NC_011916.1.
DR   AlphaFoldDB; B8GXB6; -.
DR   SMR; B8GXB6; -.
DR   PRIDE; B8GXB6; -.
DR   EnsemblBacteria; ACL95606; ACL95606; CCNA_02141.
DR   GeneID; 7330447; -.
DR   KEGG; ccs:CCNA_02141; -.
DR   PATRIC; fig|565050.3.peg.2099; -.
DR   HOGENOM; CLU_099018_2_1_5; -.
DR   OMA; DLLIMEF; -.
DR   OrthoDB; 1873899at2; -.
DR   Proteomes; UP000001364; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR35091; 1.
DR   Pfam; PF03748; FliL; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Chemotaxis; Flagellar rotation;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..205
FT                   /note="Flagellar FliL protein"
FT                   /id="PRO_0000395336"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          26..63
FT                   /note="Not required for flagellum motility, although
FT                   mutants lcaking this region swim less smoothly and are more
FT                   sensitive to O(2) deprivation"
FT   REGION          58..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        56
FT                   /note="K -> E (in Ref. 1; AAA62448)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92..101
FT                   /note="GAAGTPVIKE -> RRWDSGDQG (in Ref. 1; AAA62448)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   205 AA;  22108 MW;  4D5352FC7F29DE7C CRC64;
     MAKKPEKEAP APEGEEGAEG EAPAKKKPPI LIIAIAAGVL VLGGGGAAAF FLLKPKPAAE
     AGEHGEKKEE KKKEKKKEEK GDKKDAEKGA EGAAGTPVIK EGPDGVVFYT LPDIVVNMQT
     ADGKSTFLKL KLTFELPDEE TADELTPNLP RLQDMFQTFL RELRPEDLNG SQGTYQLRVE
     LLRRVNLVAA PAKVNAVLIE EMLIN
 
 
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