RL2_ACIB5
ID RL2_ACIB5 Reviewed; 274 AA.
AC B7IA36;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=AB57_3527;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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; CP001182; ACJ42894.1; -; Genomic_DNA.
DR RefSeq; WP_001122317.1; NC_011586.2.
DR PDB; 6V39; EM; 3.04 A; C=1-274.
DR PDB; 6V3A; EM; 2.82 A; C=1-274.
DR PDB; 6V3B; EM; 2.91 A; C=1-274.
DR PDB; 6V3D; EM; 2.95 A; C=1-274.
DR PDB; 7M4V; EM; 2.54 A; C=1-274.
DR PDB; 7M4W; EM; 2.55 A; C=1-274.
DR PDB; 7M4X; EM; 2.66 A; C=1-274.
DR PDB; 7M4Y; EM; 2.50 A; C=1-274.
DR PDB; 7M4Z; EM; 2.92 A; C=1-274.
DR PDB; 7RYF; EM; 2.65 A; C=1-274.
DR PDB; 7RYG; EM; 2.38 A; C=1-274.
DR PDB; 7RYH; EM; 2.43 A; C=1-274.
DR PDBsum; 6V39; -.
DR PDBsum; 6V3A; -.
DR PDBsum; 6V3B; -.
DR PDBsum; 6V3D; -.
DR PDBsum; 7M4V; -.
DR PDBsum; 7M4W; -.
DR PDBsum; 7M4X; -.
DR PDBsum; 7M4Y; -.
DR PDBsum; 7M4Z; -.
DR PDBsum; 7RYF; -.
DR PDBsum; 7RYG; -.
DR PDBsum; 7RYH; -.
DR AlphaFoldDB; B7IA36; -.
DR SMR; B7IA36; -.
DR IntAct; B7IA36; 2.
DR GeneID; 66395743; -.
DR KEGG; abn:AB57_06560; -.
DR HOGENOM; CLU_036235_2_1_6; -.
DR OMA; SCIELRP; -.
DR Proteomes; UP000007094; 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..274
FT /note="50S ribosomal protein L2"
FT /id="PRO_1000141490"
FT REGION 38..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:7M4V"
FT TURN 11..15
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:7M4V"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:7M4V"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:7M4V"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:7M4V"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:7M4V"
SQ SEQUENCE 274 AA; 30280 MW; 92BC04B85D2C2330 CRC64;
MPIQKCKPTS PGRRFVEKVV HDHLHKGAPY APLVEAKKRT GGRNNNGHIT TRHVGGGHKQ
HYRIVDFKRN KDGVPAVVER IEYDPNRTAH IALLKYADGE RRYIIAPKGL RAGDKVQSGN
DAPIRPGNCL PLRNMPIGST LHNVELKIGK GAQLARSAGA SVQLLGRDGS YAIIRLRSGE
MRKVHVECRA VIGEVSNQEN NLRSLGKAGA ARWRGVRPTV RGMAMNPIDH PHGGGEGRNK
GIQPVSPWGQ KAKGYKTRTN KRTTKMIIRD RRVK
