ID   RL1_CORGL               Reviewed;         236 AA.
AC   Q9LAK5;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN   Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318};
GN   OrderedLocusNames=Cgl0477, cg0564;
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=11238976; DOI=10.1099/00221287-147-3-691;
RA   Wehmeier L., Brockmann-Gretza O., Pisabarro A., Tauch A., Puhler A.,
RA   Martin J.F., Kalinowski J.;
RT   "A Corynebacterium glutamicum mutant with a defined deletion within the
RT   rplK gene is impaired in (p)ppGpp accumulation upon amino acid
RT   starvation.";
RL   Microbiology 147:691-700(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=11319098; DOI=10.1128/aem.67.5.2183-2190.2001;
RA   Barreiro C., Gonzalez-Lavado E., Martin J.F.;
RT   "Organization and transcriptional analysis of a six gene cluster around the
RT   rplK-prlA operon of Corynebacterium glutamicum encoding the ribosomal
RT   proteins L11 and L1.";
RL   Appl. Environ. Microbiol. 67:2183-2190(2001).
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=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   [4]
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: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC       the ribosome, and is involved in E site tRNA release.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of the L11 operon by binding to its mRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01318}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR   EMBL; AF130462; AAF36508.1; -; Genomic_DNA.
DR   EMBL; AJ300822; CAC38385.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB97870.1; -; Genomic_DNA.
DR   EMBL; BX927149; CAF19191.1; -; Genomic_DNA.
DR   RefSeq; NP_599722.1; NC_003450.3.
DR   RefSeq; WP_011013680.1; NC_006958.1.
DR   AlphaFoldDB; Q9LAK5; -.
DR   SMR; Q9LAK5; -.
DR   STRING; 196627.cg0564; -.
DR   KEGG; cgb:cg0564; -.
DR   KEGG; cgl:Cgl0477; -.
DR   PATRIC; fig|196627.13.peg.475; -.
DR   eggNOG; COG0081; Bacteria.
DR   HOGENOM; CLU_062853_0_0_11; -.
DR   OMA; GWTDVDV; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR   InterPro; IPR005878; Ribosom_L1_bac-type.
DR   InterPro; IPR002143; Ribosomal_L1.
DR   InterPro; IPR023674; Ribosomal_L1-like.
DR   InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_L1_CS.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; SSF56808; 1.
DR   TIGRFAMs; TIGR01169; rplA_bact; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Repressor; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Translation regulation; tRNA-binding.
FT   CHAIN           1..236
FT                   /note="50S ribosomal protein L1"
FT                   /id="PRO_0000125649"
SQ   SEQUENCE   236 AA;  25046 MW;  716A2A65EC97BDEE CRC64;
     MSKNSKAYRE AAEKIDAGRI YSPLEAANLV KETSSKNYDA SIDVAIRLGV DPRKADQLVR
     GTVSLPNGTG KTVRVAVFAQ GEKATEAEAA GADFVGTDEL VEKIQGGWTD FDVAIATPDQ
     MAKIGRIARV LGPRGLMPNP KTGTVTNDVA KAIEEVKGGK ISFRVDKASN LHAAIGKASF
     DAKKLAENYG ALLDEIIRIK PSSAKGIYVK RVTLSSTTGP GVEVDTHVTK NYAEEA