ID A0A1G8PDZ3_9BACI Unreviewed; 207 AA.
AC A0A1G8PDZ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05216352_11448 {ECO:0000313|EMBL:SDI90724.1};
OS Alteribacillus bidgolensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=930129 {ECO:0000313|EMBL:SDI90724.1, ECO:0000313|Proteomes:UP000199017};
RN [1] {ECO:0000313|EMBL:SDI90724.1, ECO:0000313|Proteomes:UP000199017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4B,CCM 7963,CECT 7998,DSM 25260,IBRC-M 10614,KCTC 13821
RC {ECO:0000313|Proteomes:UP000199017};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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.
CC {ECO:0000256|ARBA:ARBA00011838, ECO:0000256|HAMAP-Rule:MF_01328}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000256|ARBA:ARBA00010528, ECO:0000256|HAMAP-Rule:MF_01328}.
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DR EMBL; FNDU01000014; SDI90724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8PDZ3; -.
DR STRING; 930129.SAMN05216352_11448; -.
DR OrthoDB; 9803201at2; -.
DR Proteomes; UP000199017; 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:UP000199017};
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..79
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 207 AA; 22609 MW; 31829A0EEF5C0FDF CRC64;
MPKVALLNQT GSKVGDIDLA DTIFGIEPNE TVLHDAVVMH QASLRQGTHK VKNRSERRGG
GRKPWRQKGT GRARQGSIRS PQWVGGGVVF GPTPRQYSYK LPKKVRRLAI KSALSTKVKE
EAIVVVDSLQ LEAPKTKEMV NILSGLSVDE KALVVTADYN EQVALSARNI PGVTFATVDG
VNVLELLKHD KLVITQEAVE KVEEVLA
//