RL2_PORGI
ID RL2_PORGI Reviewed; 274 AA.
AC Q7MTL6;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=PG_1935;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_01320}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR EMBL; AE015924; AAQ66916.1; -; Genomic_DNA.
DR RefSeq; WP_010956448.1; NC_002950.2.
DR AlphaFoldDB; Q7MTL6; -.
DR SMR; Q7MTL6; -.
DR STRING; 242619.PG_1935; -.
DR EnsemblBacteria; AAQ66916; AAQ66916; PG_1935.
DR GeneID; 57239593; -.
DR KEGG; pgi:PG_1935; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_10; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 961486at2; -.
DR Proteomes; UP000000588; 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; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 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; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR01171; rplB_bact; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..274
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129595"
FT REGION 197..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..274
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 29717 MW; E5C6C7955E159706 CRC64;
MGIRKLKPTT PGQRHKVIGA FDKITASTPE KSLVVGKKKT GGRNNTGKMT MRYIGGGHKQ
KYRFIDFKRT KDGIPATVKT IEYDPNRSSR IALLYYADGA KAYIIAPDGL EVGHTVMSGS
EAAPEVGNAL PLANIPVGTI IHNIELRPGQ GAKMVRSAGS FAQLTSREGT YVVIKMPSGE
VRRILSTCKA TIGSVGNSDH ALEKSGKAGR SRWLGRRPHN RGVVMNPVDH PMGGGEGRQS
GGHPRSRKGL YAKGLKTRAP KKHSSKYIIE RRKK