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Database: UniProt
Entry: A0A0C3I3Q3_9VIBR
LinkDB: A0A0C3I3Q3_9VIBR
Original site: A0A0C3I3Q3_9VIBR 
ID   A0A0C3I3Q3_9VIBR        Unreviewed;       274 AA.
AC   A0A0C3I3Q3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=SU60_18390 {ECO:0000313|EMBL:KIN09665.1};
OS   Vibrio mytili.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=50718 {ECO:0000313|EMBL:KIN09665.1, ECO:0000313|Proteomes:UP000031977};
RN   [1] {ECO:0000313|EMBL:KIN09665.1, ECO:0000313|Proteomes:UP000031977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 528 {ECO:0000313|EMBL:KIN09665.1,
RC   ECO:0000313|Proteomes:UP000031977};
RA   Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra J.;
RT   "Draft genome of Vibrio mytili type strain CAIM 528.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KIN09665.1}.
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DR   EMBL; JXOK01000076; KIN09665.1; -; Genomic_DNA.
DR   RefSeq; WP_041156800.1; NZ_JXOK01000076.1.
DR   AlphaFoldDB; A0A0C3I3Q3; -.
DR   STRING; 50718.SU60_18390; -.
DR   OrthoDB; 9778722at2; -.
DR   Proteomes; UP000031977; 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   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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01320};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01320}.
FT   DOMAIN          124..252
FT                   /note="Large ribosomal subunit protein uL2 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01382"
FT   REGION          223..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   274 AA;  29928 MW;  4906F7FE74989D3C CRC64;
     MAIVKCKPTS PGRRHVVKVV NADLHKGKPY APLLEKNSKN GGRNNKGRIT VRHIGGGHKH
     HYRVVDFKRT KDGIPATVER LEYDPNRSAN IALVLYKDGE RRYILAPKGV VAGDVIQSGV
     NAPIKAGNTL PMRNIPVGST VHNVELKPGK GGQLARSAGA YAQIVARDGA YVTIRLRSGE
     MRKVLSEGRA TIGEVGNSEH MLRELGKAGA SRHRGIRPTV RGVVMNPIDH PHGGGEGRTS
     GGRHPVSPWG MPTKGFKTRK NKRTDKYIVR RRNK
//
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