GenomeNet

Database: UniProt
Entry: E3PTY0_ACESD
LinkDB: E3PTY0_ACESD
Original site: E3PTY0_ACESD 
ID   E3PTY0_ACESD            Unreviewed;       232 AA.
AC   E3PTY0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Large ribosomal subunit protein uL1 {ECO:0000256|HAMAP-Rule:MF_01318};
GN   Name=rplA {ECO:0000256|HAMAP-Rule:MF_01318,
GN   ECO:0000313|EMBL:CBH22334.1};
GN   OrderedLocusNames=CLOST_2214 {ECO:0000313|EMBL:CBH22334.1};
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH22334.1, ECO:0000313|Proteomes:UP000007041};
RN   [1] {ECO:0000313|Proteomes:UP000007041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC   {ECO:0000313|Proteomes:UP000007041};
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
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:0000256|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:0000256|HAMAP-Rule:MF_01318}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01318}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       {ECO:0000256|ARBA:ARBA00010531, ECO:0000256|HAMAP-Rule:MF_01318,
CC       ECO:0000256|RuleBase:RU000659}.
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; FP565809; CBH22334.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3PTY0; -.
DR   STRING; 1511.CLOST_2214; -.
DR   KEGG; cst:CLOST_2214; -.
DR   eggNOG; COG0081; Bacteria.
DR   HOGENOM; CLU_062853_0_0_9; -.
DR   Proteomes; UP000007041; 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; 3.30.190.20; -; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR   InterPro; IPR005878; Ribosom_uL1_bac-type.
DR   InterPro; IPR002143; Ribosomal_uL1.
DR   InterPro; IPR023674; Ribosomal_uL1-like.
DR   InterPro; IPR028364; Ribosomal_uL1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_uL1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_uL1_CS.
DR   NCBIfam; TIGR01169; rplA_bact; 1.
DR   PANTHER; PTHR36427:SF3; 39S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR36427; 54S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; Ribosomal protein L1; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007041};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_01318};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW   Rule:MF_01318}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01318}.
SQ   SEQUENCE   232 AA;  25013 MW;  0357A6538EC9E152 CRC64;
     MAKKGKKYQE ALSKFDKNNY YNATEALGVV VEVASAKFDE TVEAHIKLGV DSRHADQQVR
     GAVVLPNGTG KTNRVLVFAK GEKAKEAEAA GADFVGAEDL VTKIQSENWF DFDVIVATPD
     MMGLVGRLGR VLGPKGLMPN PKSGTVTFEV EKAINEIKAG KVEYRLDKTN IIHVPVGKVS
     FGKEKLAENF HALMEAVVKA KPSAAKGQYL RSVVVTSTMG PGVKINPARV ND
//
DBGET integrated database retrieval system