ID A0A399SW46_9BACT Unreviewed; 209 AA.
AC A0A399SW46;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000256|ARBA:ARBA00035244, ECO:0000256|HAMAP-Rule:MF_01328};
GN Name=rplD {ECO:0000256|HAMAP-Rule:MF_01328};
GN ORFNames=D1614_19640 {ECO:0000313|EMBL:RIJ46187.1};
OS Maribellus luteus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Maribellus.
OX NCBI_TaxID=2305463 {ECO:0000313|EMBL:RIJ46187.1, ECO:0000313|Proteomes:UP000265926};
RN [1] {ECO:0000313|EMBL:RIJ46187.1, ECO:0000313|Proteomes:UP000265926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XSD2 {ECO:0000313|EMBL:RIJ46187.1,
RC ECO:0000313|Proteomes:UP000265926};
RA Zhou L.Y.;
RT "Pallidiluteibacterium maritimus gen. nov., sp. nov., isolated from coastal
RT sediment.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC {ECO:0000256|HAMAP-Rule:MF_01328}.
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:0000256|HAMAP-Rule:MF_01328}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01328}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000256|ARBA:ARBA00010528, ECO:0000256|HAMAP-Rule:MF_01328}.
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:RIJ46187.1}.
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DR EMBL; QWGR01000016; RIJ46187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399SW46; -.
DR OrthoDB; 9803201at2; -.
DR Proteomes; UP000265926; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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_uL4.
DR InterPro; IPR013005; Ribosomal_uL4-like.
DR InterPro; IPR023574; Ribosomal_uL4_dom_sf.
DR NCBIfam; TIGR03953; rplD_bact; 1.
DR PANTHER; PTHR10746:SF6; 39S RIBOSOMAL PROTEIN L4, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10746; 50S RIBOSOMAL PROTEIN L4; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; Ribosomal protein L4; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000265926};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01328};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01328}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01328};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}.
FT REGION 44..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 23117 MW; 5E8095CF6187ABD4 CRC64;
MELSVLNIEG KETGRKVTLS DQIFGIEPSD HAIYLDVKQY MANQRQGTSK SKERGEIAGS
TRKIKRQKGT GTARAGSIKS PVFRGGGTIF GPRPRTYGFK LNKKVKQLAR KSALTYKASE
KSILVLEDFN FEAPKTKEMV ALKSNLQIAE KKALFVLPAE NNNIYLSSRN LQDVSVVTAS
ELNTYQILNA KTIVLCEGSV AKIEEAFKL
//
