RL2_MYCS2
ID RL2_MYCS2 Reviewed; 278 AA.
AC A0QSD4; I7G409;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320};
GN OrderedLocusNames=MSMEG_1439, MSMEI_1403;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK74446.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37876.1; -; Genomic_DNA.
DR RefSeq; WP_011727672.1; NZ_SIJM01000016.1.
DR RefSeq; YP_885822.1; NC_008596.1.
DR PDB; 5O60; EM; 3.20 A; C=1-278.
DR PDB; 5O61; EM; 3.31 A; C=1-278.
DR PDB; 5XYM; EM; 3.08 A; C=1-278.
DR PDB; 5ZEB; EM; 3.40 A; C=1-278.
DR PDB; 5ZEP; EM; 3.40 A; C=1-278.
DR PDB; 5ZET; EM; 3.20 A; C=1-278.
DR PDB; 6DZI; EM; 3.46 A; C=2-276.
DR PDB; 6DZP; EM; 3.42 A; C=1-278.
DR PDBsum; 5O60; -.
DR PDBsum; 5O61; -.
DR PDBsum; 5XYM; -.
DR PDBsum; 5ZEB; -.
DR PDBsum; 5ZEP; -.
DR PDBsum; 5ZET; -.
DR PDBsum; 6DZI; -.
DR PDBsum; 6DZP; -.
DR AlphaFoldDB; A0QSD4; -.
DR SMR; A0QSD4; -.
DR IntAct; A0QSD4; 3.
DR STRING; 246196.MSMEI_1403; -.
DR PRIDE; A0QSD4; -.
DR EnsemblBacteria; ABK74446; ABK74446; MSMEG_1439.
DR EnsemblBacteria; AFP37876; AFP37876; MSMEI_1403.
DR GeneID; 66732898; -.
DR KEGG; msg:MSMEI_1403; -.
DR KEGG; msm:MSMEG_1439; -.
DR PATRIC; fig|246196.19.peg.1425; -.
DR eggNOG; COG0090; Bacteria.
DR OMA; SCIELRP; -.
DR OrthoDB; 961486at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..278
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000309958"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..58
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:5O60"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:5O60"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5O60"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5XYM"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6DZP"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:5XYM"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:5XYM"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5ZET"
FT TURN 263..267
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5O60"
SQ SEQUENCE 278 AA; 30358 MW; 1F028C8A34842461 CRC64;
MGIRKYKPTT PGRRGASVSD FAEITRSTPE KSLVRPLHGK GGRNAHGRIT TRHKGGGHKR
AYRVIDFRRH DKDGVNAKVA HIEYDPNRTA NIALLHYLDG EKRYIIAPQG LKQGDVIESG
ANADIKPGNN LPLRNIPAGT VIHAVELRPG GGAKLARSAG VSIQLLGKEG TYAALRMPSG
EIRRVDVRCR ATVGEVGNAE QSNINWGKAG RMRWKGKRPT VRGVVMNPVD HPHGGGEGKT
SGGRHPVSPW GKPEGRTRKP NKPSDKLIVR RRRTGKKR
