RL1_PECCP
ID RL1_PECCP Reviewed; 234 AA.
AC C6DHR2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=PC1_0202;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001657; ACT11262.1; -; Genomic_DNA.
DR RefSeq; WP_012772933.1; NC_012917.1.
DR AlphaFoldDB; C6DHR2; -.
DR SMR; C6DHR2; -.
DR STRING; 561230.PC1_0202; -.
DR EnsemblBacteria; ACT11262; ACT11262; PC1_0202.
DR KEGG; pct:PC1_0202; -.
DR eggNOG; COG0081; Bacteria.
DR HOGENOM; CLU_062853_0_0_6; -.
DR OMA; GWTDVDV; -.
DR OrthoDB; 1671455at2; -.
DR Proteomes; UP000002736; Chromosome.
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..234
FT /note="50S ribosomal protein L1"
FT /id="PRO_1000214428"
SQ SEQUENCE 234 AA; 24707 MW; 46B21A5F759A4907 CRC64;
MAKLTKRMRV IRDKVDVTKQ YDINEAVALL KELATAKFVE SVDVAVNLGI DARKSDQNVR
GATVLPHGTG RSVRVAVFTQ GANAEAAKAA GAEFVGMEDL AEQIKKGEMG FDVVIASPDA
MRVVGQLGQV LGPRGLMPNP KVGTVTPNVA EAVNNAKAGQ VRYRNDKNGI IHTTIGKVDF
DSNKLKENLE ALLVALKKAK PSQAKGVYIK KVSLSTTMGA GVAVDQSGLN AAAN