ID A0A427DSL5_9PSED Unreviewed; 211 AA.
AC A0A427DSL5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=EGJ27_16900 {ECO:0000313|EMBL:RRV06345.1};
OS Pseudomonas sp. v388.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2479849 {ECO:0000313|EMBL:RRV06345.1, ECO:0000313|Proteomes:UP000268166};
RN [1] {ECO:0000313|EMBL:RRV06345.1, ECO:0000313|Proteomes:UP000268166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=v388 {ECO:0000313|Proteomes:UP000268166};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-2018) 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 -!- PTM: Methylated by PrmB. {ECO:0000256|HAMAP-Rule:MF_01325}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRV06345.1}.
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DR EMBL; RHQN01000006; RRV06345.1; -; Genomic_DNA.
DR RefSeq; WP_044321452.1; NZ_RHQN01000006.1.
DR AlphaFoldDB; A0A427DSL5; -.
DR OrthoDB; 9806135at2; -.
DR Proteomes; UP000268166; Unassembled WGS sequence.
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 Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_01325}; Reference proteome {ECO:0000313|Proteomes:UP000268166};
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 MOD_RES 150
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01325"
SQ SEQUENCE 211 AA; 22563 MW; 8F5539911B2A1CB6 CRC64;
MTIGVVGRKC GMTRIFTEEG VSIPVTVIEI EPNRVTQFKT EETDGYRAVQ VTVGERRASR
VTAAQAGHFA KANVAAGRAV MEFRLEEGDY QAGDQINAEI FAAGQLVDVT GQSKGKGFQG
TIKRWNFRGQ DNTHGNSVSH RVPGSIGQCQ TPGRVFKGKK MSGHMGAERV TVQSLEVVRV
DAERNLLLVK GAVPGATGGN LVVRPAAKAR G
//
