ID   A0A0G1NWC8_9BACT        Unreviewed;       280 AA.
AC   A0A0G1NWC8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 30.
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=UW89_C0007G0007 {ECO:0000313|EMBL:KKT88464.1};
OS   Parcubacteria group bacterium GW2011_GWB1_45_10.
OC   Bacteria.
OX   NCBI_TaxID=1618877 {ECO:0000313|EMBL:KKT88464.1, ECO:0000313|Proteomes:UP000033817};
RN   [1] {ECO:0000313|EMBL:KKT88464.1, ECO:0000313|Proteomes:UP000033817}
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:KKT88464.1}.
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DR   EMBL; LCKC01000007; KKT88464.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1NWC8; -.
DR   STRING; 1618877.UW89_C0007G0007; -.
DR   PATRIC; fig|1618877.3.peg.253; -.
DR   Proteomes; UP000033817; 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          124..253
FT                   /note="Large ribosomal subunit protein uL2 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01382"
FT   REGION          222..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   280 AA;  31416 MW;  3A154575427E5A86 CRC64;
     MAIKTAKPKT PGRRHYQVID YSFLSKTGPY KPLLSSKKKT GGRNNRGRIT MRHQGGGAKQ
     MYRLVEFGQG FLGQKARVET IEYDPNRTAF ICLVVVENGK RCYILAPANV KVGDTIEIAE
     KTEFKPGNRM KLKNIPVGTQ VHNIELRPGQ KGRLARSAGS FAVVMAHEGK YATLKMPSSE
     IRKVSVESFA SIGQVSNFER RLISWGKAGR SRLRGIRPTV RGKVMNPRDH PYGGGEGKTT
     RGTKRPKDKW GNITGGKKTR NKKKWSSKFI MQRRIKTKKS
//