ID F3L617_9GAMM Unreviewed; 259 AA.
AC F3L617;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=IMCC3088_654 {ECO:0000313|EMBL:EGG28224.1};
OS Aequoribacter fuscus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Aequoribacter.
OX NCBI_TaxID=2518989 {ECO:0000313|EMBL:EGG28224.1, ECO:0000313|Proteomes:UP000005615};
RN [1] {ECO:0000313|EMBL:EGG28224.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG28224.1};
RX PubMed=21551310; DOI=10.1128/JB.05111-11;
RA Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.;
RT "Genome sequence of strain IMCC3088, a proteorhodopsin-containing marine
RT bacterium belonging to the OM60/NOR5 clade.";
RL J. Bacteriol. 193:3415-3416(2011).
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:EGG28224.1}.
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DR EMBL; AEIG01000147; EGG28224.1; -; Genomic_DNA.
DR AlphaFoldDB; F3L617; -.
DR STRING; 2518989.IMCC3088_654; -.
DR eggNOG; COG0090; Bacteria.
DR Proteomes; UP000005615; 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 Reference proteome {ECO:0000313|Proteomes:UP000005615};
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 108..236
FT /note="Large ribosomal subunit protein uL2 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01382"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 259 AA; 28219 MW; 8EA0590B8E9789EB CRC64;
MRVVEQDLHK GAPHKPLLES QSKSGGRNNN GRITTRHVGG GHKQHYRIID FKRNKDGMPA
KVERLEYDPN RTSHIALILF PDGERRYILA PKGLKAGDVV QNGPAAPIKA GNCLPIRNIP
VGSVIHAIEL KPGKGAQLAR SAGAAVQLVA REGAYATIRL RSGEMRKVLS DCRATIGEVS
NSEHSLRKLG KAGAKRWRGV RPTVRGVAMN PVDHPHGGGE GRTSGGRHPV SPWGTPTKGY
KTRSNKRTDK LIVRRRGKK
//
