ID U5SF03_9LACT Unreviewed; 277 AA.
AC U5SF03;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000256|HAMAP-Rule:MF_01320,
GN ECO:0000313|EMBL:AGY82673.1};
GN ORFNames=Q783_11005 {ECO:0000313|EMBL:AGY82673.1};
OS Carnobacterium inhibens subsp. gilichinskyi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY82673.1, ECO:0000313|Proteomes:UP000017469};
RN [1] {ECO:0000313|EMBL:AGY82673.1, ECO:0000313|Proteomes:UP000017469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN1359 {ECO:0000313|EMBL:AGY82673.1,
RC ECO:0000313|Proteomes:UP000017469};
RX PubMed=24285647;
RA Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT (DSM 27470T).";
RL Genome Announc. 1:e00985-13(2013).
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}.
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DR EMBL; CP006812; AGY82673.1; -; Genomic_DNA.
DR RefSeq; WP_023179563.1; NC_022606.1.
DR AlphaFoldDB; U5SF03; -.
DR STRING; 1266845.Q783_11005; -.
DR KEGG; caw:Q783_11005; -.
DR PATRIC; fig|1266845.5.peg.2098; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_9; -.
DR Proteomes; UP000017469; Chromosome.
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..253
FT /note="Large ribosomal subunit protein uL2 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01382"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 30111 MW; DCCC85883A076D3C CRC64;
MGIKKYKPTT NGRRNMTGSD FAEITSTTPE KTLLEPNKRK AGRNNAGKIM VRHRGGGHKR
NYRVIDFKRN KDGIVGIIKT VEYDPNRSAN IALVQYTDGV KTYIIAPKGI QVGQQIISGE
TVDIKTGNAL LLENIPAGTV IHNIEMKPGK GGQLVRSAGT SAQVLGKEGK YVMIRLNSGE
VRLILGTCRA TIGSVGNEQH ELINIGKAGR SRWLGKRPTV RGSVMNPNDH PHGGGEGKAP
IGHAGPMTPW GKPALGLKTR NKKAQSNKFI TRRRKTK
//
