RL2_MYCBO
ID RL2_MYCBO Reviewed; 280 AA.
AC O06047; A0A1R3XX63; X2BFW0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320};
GN OrderedLocusNames=BQ2027_MB0724;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCG;
RX PubMed=9402018; DOI=10.1046/j.1365-2958.1997.5811946.x;
RA Sander P., Prammananan T., Meier A., Frischkorn K., Boettger E.C.;
RT "The role of ribosomal RNAs in macrolide resistance.";
RL Mol. Microbiol. 26:469-480(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; Y13228; CAA73675.1; -; Genomic_DNA.
DR EMBL; LT708304; SIT99323.1; -; Genomic_DNA.
DR RefSeq; NP_854382.1; NC_002945.3.
DR RefSeq; WP_003403582.1; NC_002945.4.
DR AlphaFoldDB; O06047; -.
DR SMR; O06047; -.
DR EnsemblBacteria; SIT99323; SIT99323; BQ2027_MB0724.
DR GeneID; 45424669; -.
DR PATRIC; fig|233413.5.peg.790; -.
DR OMA; SCIELRP; -.
DR Proteomes; UP000001419; 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 Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..280
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129578"
FT REGION 27..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..59
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 20
FT /note="D -> Y (in Ref. 1; CAA73675)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="A -> P (in Ref. 1; CAA73675)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="G -> A (in Ref. 1; CAA73675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 30577 MW; 456837947E32FFBB CRC64;
MAIRKYKPTT PGRRGASVSD FAEITRSTPE KSLVRPLHGR GGRNAHGRIT TRHKGGGHKR
AYRMIDFRRN DKDGVNAKVA HIEYDPNRTA RIALLHYLDG EKRYIIAPNG LSQGDVVESG
ANADIKPGNN LPLRNIPAGT LIHAVELRPG GGAKLARSAG SSIQLLGKEA SYASLRMPSG
EIRRVDVRCR ATVGEVGNAE QANINWGKAG RMRWKGKRPS VRGVVMNPVD HPHGGGEGKT
SGGRHPVSPW GKPEGRTRNA NKSSNKFIVR RRRTGKKHSR
