ID A0A094P9V5_9ACTN Unreviewed; 278 AA.
AC A0A094P9V5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000256|HAMAP-Rule:MF_01320};
GN ORFNames=GM46_10620 {ECO:0000313|EMBL:KGA06279.1};
OS actinobacterium acAcidi.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA06279.1, ECO:0000313|Proteomes:UP000029305};
RN [1] {ECO:0000313|EMBL:KGA06279.1, ECO:0000313|Proteomes:UP000029305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the primary rRNA binding proteins. Required for
CC association of the 30S and 50S subunits to form the 70S ribosome, for
CC tRNA binding and peptide bond formation. It has been suggested to have
CC peptidyltransferase activity; this is somewhat controversial. Makes
CC several contacts with the 16S rRNA in the 70S ribosome.
CC {ECO:0000256|HAMAP-Rule:MF_01320}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC subunit in the 70S ribosome. {ECO:0000256|HAMAP-Rule:MF_01320}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000256|ARBA:ARBA00005636, ECO:0000256|HAMAP-Rule:MF_01320}.
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:KGA06279.1}.
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DR EMBL; JNSG01000105; KGA06279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094P9V5; -.
DR PATRIC; fig|1504320.4.peg.2135; -.
DR Proteomes; UP000029305; Unassembled WGS sequence.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 4.10.950.10; Ribosomal protein L2, domain 3; 1.
DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR002171; Ribosomal_uL2.
DR InterPro; IPR005880; Ribosomal_uL2_bac/org-type.
DR InterPro; IPR022669; Ribosomal_uL2_C.
DR InterPro; IPR022671; Ribosomal_uL2_CS.
DR InterPro; IPR014726; Ribosomal_uL2_dom3.
DR InterPro; IPR022666; Ribosomal_uL2_RNA-bd_dom.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR NCBIfam; TIGR01171; rplB_bact; 1.
DR PANTHER; PTHR13691:SF5; 39S RIBOSOMAL PROTEIN L2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13691; RIBOSOMAL PROTEIN L2; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01320};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01320}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01320};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01320}.
FT DOMAIN 124..252
FT /note="Large ribosomal subunit protein uL2 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01382"
FT REGION 212..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 278 AA; 30559 MW; C20A475C80375BEA CRC64;
MGIRKRKPTS AGRRFQTVSD FADITKSTPE KSLLAKKTSA GGRNVYGRVT SRHQGGGHKQ
QYRIIDFKRN YDQYEAKVAA IEYDPNRTCR IALLHYADGS KAYILAPKGL EVGMRVQSGP
KADIKVGNAL PLRYLPVGTV VHNIELRPGQ GGKVGRSAGM AVQLVAKEGD FATLRMPSSE
MRRVPIDCRA TIGEVGNAEH ELIKIGKAGR NRWKGVRPQS RGVVMNPVDH PHGGGEGKTS
GGRHPVSPWG KPERRTRNKN KSSQQLIVRR RRSGKGRA
//