ID RL2_ANAMF Reviewed; 277 AA.
AC B9KJ67;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000255|HAMAP-Rule:MF_01320};
DE AltName: Full=50S ribosomal protein L2 {ECO:0000305};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=AMF_693;
OS Anaplasma marginale (strain Florida).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=320483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Florida;
RX PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT "Conservation in the face of diversity: multistrain analysis of an
RT intracellular bacterium.";
RL BMC Genomics 10:16-16(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; CP001079; ACM49529.1; -; Genomic_DNA.
DR RefSeq; WP_010265300.1; NZ_AFMS01000137.1.
DR AlphaFoldDB; B9KJ67; -.
DR SMR; B9KJ67; -.
DR STRING; 320483.AMF_693; -.
DR GeneID; 7397875; -.
DR KEGG; amf:AMF_693; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_5; -.
DR Proteomes; UP000007307; 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; Nucleic acid-binding proteins; 1.
DR Gene3D; 4.10.950.10; Ribosomal protein L2, domain 3; 1.
DR HAMAP; MF_01320_B; Ribosomal_uL2_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; IPR022671; Ribosomal_uL2_CS.
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.
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..277
FT /note="Large ribosomal subunit protein uL2"
FT /id="PRO_1000165716"
FT REGION 225..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..277
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 29736 MW; 829C1270BAC50FEB CRC64;
MSLKVLNPVT PSLRGTVMVN RVALWRGKPE KSLVVGRVSS GGRNAHGVIT VRHRGGGHKR
LHRVVDLKRN KDGVQAVVQR LEYDPNRTAF LALVRYEDGE LSYILAPDGL KVSDVVVSGV
GSDVLPGNCL QLGSIPAGTF VHNVELRPCG GGIIARAAGS YAQVMGRDGA YVLLRLGSGE
VRKILALCRA TVGVVSNLNN QNIKLGKAGR NRWLGFRPTV RGVAMNPVDH PHGGGEGKTS
GGRNSVTPWG VPTKGKKTRK RGKHSDKYIK VSSVRKR
//
