ID   RL4_CAMHC               Reviewed;         204 AA.
AC   A7HZK7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328};
GN   OrderedLocusNames=CHAB381_0085;
OS   Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS   CH001A).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360107;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT   commensal isolated from the human gastrointestinal tract.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000776; ABS51910.1; -; Genomic_DNA.
DR   RefSeq; WP_011991545.1; NC_009714.1.
DR   AlphaFoldDB; A7HZK7; -.
DR   SMR; A7HZK7; -.
DR   STRING; 360107.CHAB381_0085; -.
DR   EnsemblBacteria; ABS51910; ABS51910; CHAB381_0085.
DR   KEGG; cha:CHAB381_0085; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_2_7; -.
DR   OMA; PQVHILE; -.
DR   OrthoDB; 1572673at2; -.
DR   Proteomes; UP000002407; Chromosome.
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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..204
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000052376"
FT   REGION          49..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  22412 MW;  0BF74CA994EDEF6D CRC64;
     MSKVKVLNEK LEKASELELP ANFADVNPHN LYLYVKSYLA SLRANTANTK GRSEVSGGGK
     KPWRQKGRGG ARAGSTRTNV WVGGAVAFGP TNNRNYFQKV NKKQKRLALE FALNEKAQND
     KIFAVDSLEI SSGKTKDAAK FIKNLGVRDA LIVKNELDSA TLLAYRNLNN CYVIDINELN
     AYLVAVYSAV IIETSALQSI VKEG