ID U5P1F4_9STRE Unreviewed; 208 AA.
AC U5P1F4; U5PAM9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000256|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000256|HAMAP-Rule:MF_01325};
GN ORFNames=N597_09820 {ECO:0000313|EMBL:AGY37378.1};
OS Streptococcus ilei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1156431 {ECO:0000313|EMBL:AGY37378.1, ECO:0000313|Proteomes:UP000017124};
RN [1] {ECO:0000313|EMBL:AGY37378.1, ECO:0000313|Proteomes:UP000017124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I-P16 {ECO:0000313|Proteomes:UP000017124};
RA Hyun D.-W.;
RT "Genome sequence of Streptococcus SP. I-P16 isolated from human ileal
RT fluid.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01325,
CC ECO:0000256|RuleBase:RU003906}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L19. {ECO:0000256|HAMAP-Rule:MF_01325,
CC ECO:0000256|RuleBase:RU003906}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000256|ARBA:ARBA00006540, ECO:0000256|HAMAP-Rule:MF_01325,
CC ECO:0000256|RuleBase:RU003905}.
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DR EMBL; CP006776; AGY37378.1; -; Genomic_DNA.
DR RefSeq; WP_003010846.1; NZ_QSTR01000004.1.
DR STRING; 1156433.N597_09820; -.
DR GeneID; 75174447; -.
DR KEGG; sig:N596_07925; -.
DR KEGG; sip:N597_09820; -.
DR PATRIC; fig|1156433.3.peg.1926; -.
DR HOGENOM; CLU_044142_4_1_9; -.
DR Proteomes; UP000017124; Chromosome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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 Gene3D; 3.30.160.810; -; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR InterPro; IPR000597; Ribosomal_uL3.
DR InterPro; IPR019927; Ribosomal_uL3_bac/org-type.
DR InterPro; IPR019926; Ribosomal_uL3_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR03625; L3_bact; 1.
DR PANTHER; PTHR11229:SF8; 39S RIBOSOMAL PROTEIN L3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11229; 50S RIBOSOMAL PROTEIN L3; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW ECO:0000256|RuleBase:RU003906};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW ECO:0000256|RuleBase:RU003906}.
FT REGION 124..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 208 AA; 22236 MW; 68F49F22C37ED1B6 CRC64;
MTKGILGKKV GMTQIFTEAG ELIPVTVIEA TPNVVLQVKT VETDGYNAIQ VGFDDKREVL
SNKPAKGHVA KANTAPKRFI REFKNVEGLE VGAEITVDTF EAGDIVDVTG TSKGKGFQGV
IKRHGQSRGP MAHGSRYHRR PGSMGPVAPN RVFKGKNLAG RMGGDRVTIQ NLEVVQVVPE
KNVILIKGNV PGAKKSLITI KSAVKAGK
//
