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Database: UniProt
Entry: A0A0G1MSY9_9BACT
LinkDB: A0A0G1MSY9_9BACT
Original site: A0A0G1MSY9_9BACT 
ID   A0A0G1MSY9_9BACT        Unreviewed;       284 AA.
AC   A0A0G1MSY9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 27.
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=UW70_C0039G0030 {ECO:0000313|EMBL:KKT75099.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWA2_44_7.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619057 {ECO:0000313|EMBL:KKT75099.1, ECO:0000313|Proteomes:UP000034415};
RN   [1] {ECO:0000313|EMBL:KKT75099.1, ECO:0000313|Proteomes:UP000034415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKT75099.1}.
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DR   EMBL; LCJI01000039; KKT75099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1MSY9; -.
DR   STRING; 1619057.UW70_C0039G0030; -.
DR   PATRIC; fig|1619057.3.peg.763; -.
DR   Proteomes; UP000034415; 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; 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.
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          125..254
FT                   /note="Large ribosomal subunit protein uL2 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01382"
FT   REGION          209..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   284 AA;  31724 MW;  2FC714DCE85162B7 CRC64;
     MGIKKVKGTT PARRQMSVST FEEVTAKKPL QRLLLTKKRG SGRNNTGRIT VRHRGGGSKT
     HYRMVDFKQT DNLGVEGRVA SVEYDPNRNA YIILVNYKNG DKRYHLAPEK IGVNDHVITD
     HKTKIKTGNR CLIENIPVGF TIYNIELQKG KGGQIVRSAG TSAKLVSLEG EMAQVELPSK
     EVRFIPKGNF ASIGVVSNSD FSNIKWGKAG RTRQRGRRPQ VRGKVMNPVD HPHGGGEGRN
     SIGLKYPKTP WGLPALGVKT RKRKARTNIY RIRDRKGKNF IKTT
//
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