RL4_VIBC3
ID RL4_VIBC3 Reviewed; 200 AA.
AC A5F548; C3LXJ4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328};
GN OrderedLocusNames=VC0395_A2173, VC395_2708;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC initially binds near the 5'-end of the 23S rRNA. It is important during
CC the early stages of 50S assembly. It makes multiple contacts with
CC different domains of the 23S rRNA in the assembled 50S subunit and
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}.
CC -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC {ECO:0000255|HAMAP-Rule:MF_01328}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01328}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000255|HAMAP-Rule:MF_01328}.
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DR EMBL; CP000627; ABQ19504.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10694.1; -; Genomic_DNA.
DR RefSeq; WP_000422344.1; NZ_JAACZH010000007.1.
DR AlphaFoldDB; A5F548; -.
DR SMR; A5F548; -.
DR STRING; 345073.VC395_2708; -.
DR EnsemblBacteria; ABQ19504; ABQ19504; VC0395_A2173.
DR GeneID; 57990982; -.
DR GeneID; 66938519; -.
DR KEGG; vco:VC0395_A2173; -.
DR KEGG; vcr:VC395_2708; -.
DR PATRIC; fig|345073.21.peg.2608; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_6; -.
DR OMA; PQVHILE; -.
DR Proteomes; UP000000249; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR InterPro; IPR002136; Ribosomal_L4/L1e.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR InterPro; IPR013005; Ribosomal_uL4/L1e.
DR PANTHER; PTHR10746; PTHR10746; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; SSF52166; 1.
DR TIGRFAMs; TIGR03953; rplD_bact; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..200
FT /note="50S ribosomal protein L4"
FT /id="PRO_1000073274"
FT REGION 42..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 200 AA; 21868 MW; 33566D2E0D9193D8 CRC64;
MELMVKGANA LTVSETTFGR EFNEALVHQV VVAYAAGARQ GTRAQKTRSE VSGGGAKPWR
QKGTGRARAG TIRSPIWRTG GVTFAAKPQD HSQKVNKKMY RGAMKSILSE LVRQERLIVV
ENFSVEAPKT KALVAKLKEL ELNDVLIVTG EVDENLFLAA RNLYKVDVRD VTGIDPVSLI
AFDKVLMTAA AVKQVEEMLA
