ID   LPL_CORGL               Reviewed;          22 AA.
AC   P42456;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=leu leader peptide;
DE   AltName: Full=leuA operon attenuator peptide;
GN   Name=leuL; OrderedLocusNames=Cgl0248.1, cg0303.1;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=8117072; DOI=10.1128/aem.60.1.133-140.1994;
RA   Patek M., Krumbach K., Eggeling L., Sahm H.;
RT   "Leucine synthesis in Corynebacterium glutamicum: enzyme activities,
RT   structure of leuA, and effect of leuA inactivation on lysine synthesis.";
RL   Appl. Environ. Microbiol. 60:133-140(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- FUNCTION: Involved in control of the biosynthesis of leucine.
CC       {ECO:0000250}.
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DR   EMBL; X70959; CAA50295.1; ALT_TERM; Genomic_DNA.
DR   EMBL; BA000036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX927148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; I40725; I40725.
DR   AlphaFoldDB; P42456; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leader peptide; Leucine biosynthesis; Reference proteome.
FT   PEPTIDE         1..22
FT                   /note="leu leader peptide"
FT                   /id="PRO_0000043994"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   22 AA;  2535 MW;  BB6E3DA8604AD7F8 CRC64;
     MLHHMTSRAN LLLLRRGGSQ RS