RL3_RICPR
ID RL3_RICPR Reviewed; 216 AA.
AC P48952;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=RP659;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC STRAIN=Madrid E;
RX PubMed=8892818; DOI=10.1128/jb.178.21.6192-6199.1996;
RA Syvaenen A.-C., Amiri H., Jamal A., Andersson S.G.E., Kurland C.G.;
RT "A chimeric disposition of the elongation factor genes in Rickettsia
RT prowazekii.";
RL J. Bacteriol. 178:6192-6199(1996).
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 -!- PTM: Methylated by PrmB. {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; AJ235272; CAA15099.1; -; Genomic_DNA.
DR EMBL; Z54170; CAA90883.1; -; Genomic_DNA.
DR PIR; A71672; A71672.
DR RefSeq; NP_221023.1; NC_000963.1.
DR RefSeq; WP_004596199.1; NC_000963.1.
DR AlphaFoldDB; P48952; -.
DR SMR; P48952; -.
DR STRING; 272947.RP659; -.
DR EnsemblBacteria; CAA15099; CAA15099; CAA15099.
DR GeneID; 57569784; -.
DR KEGG; rpr:RP659; -.
DR PATRIC; fig|272947.5.peg.681; -.
DR eggNOG; COG0087; Bacteria.
DR HOGENOM; CLU_044142_2_0_5; -.
DR OMA; KRMAGRY; -.
DR Proteomes; UP000002480; 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 Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..216
FT /note="50S ribosomal protein L3"
FT /id="PRO_0000077147"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ SEQUENCE 216 AA; 23652 MW; 10F07EEFB39C287D CRC64;
MRTGIIAQKV GMTSVFNDKG ERISLTLVKV DDCQVVGHKT LAKHGYNALV IGVKDQKISK
VTKPMKQVFA NAKIAPKTKL KEFRISEDNF IDIASILEVD HFRVGQFVDI TATTIGKGFA
GSMKRHNFRG LEASHGVSIS HRSHGSTGQR QDPGKVFKGK KMAGHMGCNK VTIQNLKIFA
VDTNRKLIMI QGSIPGHKNS YLLVKDAIKK AAITIA
