ID W6TGY8_HOLOB Unreviewed; 282 AA.
AC W6TGY8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000256|HAMAP-Rule:MF_01320};
GN ORFNames=P618_200599 {ECO:0000313|EMBL:ETZ07205.1};
OS Holospora obtusa F1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales; Holosporaceae;
OC Holospora.
OX NCBI_TaxID=1399147 {ECO:0000313|EMBL:ETZ07205.1, ECO:0000313|Proteomes:UP000019112};
RN [1] {ECO:0000313|EMBL:ETZ07205.1, ECO:0000313|Proteomes:UP000019112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F1 {ECO:0000313|EMBL:ETZ07205.1,
RC ECO:0000313|Proteomes:UP000019112};
RX PubMed=25115770;
RA Dohra H., Tanaka K., Suzuki T., Fujishima M., Suzuki H.;
RT "Draft genome sequences of three Holospora species (Holospora obtusa,
RT Holospora undulata, and Holospora elegans), endonuclear symbiotic bacteria
RT of the ciliate Paramecium caudatum.";
RL FEMS Microbiol. Lett. 359:16-18(2014).
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:0000256|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:0000256|HAMAP-Rule:MF_01320}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000256|ARBA:ARBA00005636, ECO:0000256|HAMAP-Rule:MF_01320}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETZ07205.1}.
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DR EMBL; AWTR02000059; ETZ07205.1; -; Genomic_DNA.
DR RefSeq; WP_021827271.1; NZ_AWTR02000059.1.
DR AlphaFoldDB; W6TGY8; -.
DR STRING; 1399147.P618_200599; -.
DR eggNOG; COG0090; Bacteria.
DR OrthoDB; 9778722at2; -.
DR Proteomes; UP000019112; Unassembled WGS sequence.
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_L2_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 {ECO:0000313|Proteomes:UP000019112};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01320};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01320};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01320};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01320}.
FT DOMAIN 130..258
FT /note="Large ribosomal subunit protein uL2 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01382"
FT REGION 228..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..282
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 30994 MW; 8A70AE9640BABDE6 CRC64;
MSLKYYNPTS PGRRGLISLD RSELWHGRPE KSLVCFKKRT GGRNFQGRVT CRSRGGGTRP
LYRIVDFNRD HGGKGVVASR VERLEYDPNR SAFLALLSSG EVKNAPLSYI VASSGMKVGN
VVYSGEGCEI REGNSLPLAR IPSGTFVYNV ELKIGKGAQI ARSAGTYAQV MGKDLEYVLV
RLPSGEVRKI HKNCWATIGV VSNADHRNIC LAKAGRSRWL GRRPHVRGVA MNPVDHPLGG
GEGRTSGGRH PVSPKGQNSK GLRTRSRRKS RSSKMIVSRR KK
//
