ID   RL1_CAMJR               Reviewed;         233 AA.
AC   Q5HVZ2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN   Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=CJE0525;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
CC   -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC       the ribosome, and is involved in E site tRNA release.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of the L11 operon by binding to its mRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01318}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000025; AAW35112.1; -; Genomic_DNA.
DR   RefSeq; WP_002854928.1; NC_003912.7.
DR   AlphaFoldDB; Q5HVZ2; -.
DR   SMR; Q5HVZ2; -.
DR   KEGG; cjr:CJE0525; -.
DR   HOGENOM; CLU_062853_0_0_7; -.
DR   OMA; GWTDVDV; -.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR   InterPro; IPR005878; Ribosom_L1_bac-type.
DR   InterPro; IPR002143; Ribosomal_L1.
DR   InterPro; IPR023674; Ribosomal_L1-like.
DR   InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_L1_CS.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; SSF56808; 1.
DR   TIGRFAMs; TIGR01169; rplA_bact; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   3: Inferred from homology;
KW   Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   Translation regulation; tRNA-binding.
FT   CHAIN           1..233
FT                   /note="50S ribosomal protein L1"
FT                   /id="PRO_0000230597"
SQ   SEQUENCE   233 AA;  25047 MW;  A91DC3DF0B71F03B CRC64;
     MAKIAKRLKE LSQKIDSNKE YALSDAIDTI KTLKSAKFDE TVEIALKLNV DPRHADQMVR
     GSVVLPAGTG KKVRVAVIAK DAKADEAKNA GADIVGSDDL VEEIQKGNMN FDVLIATPNL
     MGLVGKVGRI LGPKGLMPNP KTGTVTMDVA QAVNNAKSGQ VNFRVDKQGN IHAGLGKVSF
     SKEQLWDNVS TFVKAINKHK PAAAKGRYIK NAALSLTMSP SVKLETQELL DMK