RL11_CORGL
ID RL11_CORGL Reviewed; 145 AA.
AC Q9LAK6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736};
GN OrderedLocusNames=Cgl0476, cg0563;
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: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit.
CC Interacts with L10 and the large rRNA to form the base of the stalk.
CC L10 forms an elongated spine to which L12 dimers bind in a sequential
CC fashion forming a multimeric L10(L12)X complex. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- PTM: One or more lysine residues are methylated. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR EMBL; AF130462; AAF36507.1; -; Genomic_DNA.
DR EMBL; AJ300822; CAC38384.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB97869.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19190.1; -; Genomic_DNA.
DR RefSeq; NP_599721.1; NC_003450.3.
DR RefSeq; WP_011013679.1; NC_006958.1.
DR AlphaFoldDB; Q9LAK6; -.
DR SMR; Q9LAK6; -.
DR STRING; 196627.cg0563; -.
DR KEGG; cgb:cg0563; -.
DR KEGG; cgl:Cgl0476; -.
DR PATRIC; fig|196627.13.peg.474; -.
DR eggNOG; COG0080; Bacteria.
DR HOGENOM; CLU_074237_2_1_11; -.
DR OMA; CKQFNAK; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR006519; Ribosomal_L11_bac-typ.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR TIGRFAMs; TIGR01632; L11_bact; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 3: Inferred from homology;
KW Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..145
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000104278"
SQ SEQUENCE 145 AA; 15330 MW; 09FBD8EE42DC0EA1 CRC64;
MAPKKKKKVT GLIKLQIQAG QANPAPPVGP ALGAHGVNIM EFCKAYNAAT ENQRGNVVPV
EITVYEDRSF DFKLKTPPAA KLLLKAAGLQ KGSGVPHTQK VGKVSMAQVR EIAETKKEDL
NARDIDAAAK IIAGTARSMG ITVEG
