RL3_ACHLI
ID RL3_ACHLI Reviewed; 212 AA.
AC A9NED3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=ACL_0087;
OS Acholeplasma laidlawii (strain PG-8A).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Acholeplasma.
OX NCBI_TaxID=441768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-8A;
RX PubMed=21784942; DOI=10.1128/jb.05059-11;
RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA Ladygina V.G., Govorun V.M.;
RT "Complete genome and proteome of Acholeplasma laidlawii.";
RL J. Bacteriol. 193:4943-4953(2011).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L19. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR EMBL; CP000896; ABX80713.1; -; Genomic_DNA.
DR RefSeq; WP_012242044.1; NC_010163.1.
DR AlphaFoldDB; A9NED3; -.
DR SMR; A9NED3; -.
DR STRING; 441768.ACL_0087; -.
DR EnsemblBacteria; ABX80713; ABX80713; ACL_0087.
DR GeneID; 66293086; -.
DR KEGG; acl:ACL_0087; -.
DR eggNOG; COG0087; Bacteria.
DR HOGENOM; CLU_044142_4_1_14; -.
DR OMA; KRMAGRY; -.
DR OrthoDB; 1270636at2; -.
DR Proteomes; UP000008558; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F: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 HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11229; PTHR11229; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR TIGRFAMs; TIGR03625; L3_bact; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..212
FT /note="50S ribosomal protein L3"
FT /id="PRO_1000086423"
FT REGION 117..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 212 AA; 22875 MW; 7A0AB94FD20CF590 CRC64;
MAKGILGRKI GMTQIFDENG VLIPVTVIDV EGNVVLQQKT VEVDGYQATQ VGFESKREKL
SNKPELGHVK KANTAPKRFV KEIRFDALNN ELLALEVGTE IKADLFTAGE DVDVTGTSKG
KGFQGNIKRH NQSRGPMTHG SRYHRGVGSL GAIKGNMKGK NLPGQMGNEQ VTVQNLKIVA
VDTENDLLLV SGSVPGPRKG YVVVRSAIKK GN