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RL1_ENTFA
ID   RL1_ENTFA               Reviewed;         229 AA.
AC   Q830Q6;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN   Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=EF_2718;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO82420.1; -; Genomic_DNA.
DR   RefSeq; NP_816350.1; NC_004668.1.
DR   RefSeq; WP_002356425.1; NZ_KE136528.1.
DR   PDB; 7P7R; EM; 2.90 A; F=1-229.
DR   PDBsum; 7P7R; -.
DR   AlphaFoldDB; Q830Q6; -.
DR   SMR; Q830Q6; -.
DR   STRING; 226185.EF_2718; -.
DR   EnsemblBacteria; AAO82420; AAO82420; EF_2718.
DR   GeneID; 60894705; -.
DR   KEGG; efa:EF2718; -.
DR   PATRIC; fig|226185.45.peg.849; -.
DR   eggNOG; COG0081; Bacteria.
DR   HOGENOM; CLU_062853_0_0_9; -.
DR   OMA; GWTDVDV; -.
DR   Proteomes; UP000001415; 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   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Repressor; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation;
KW   tRNA-binding.
FT   CHAIN           1..229
FT                   /note="50S ribosomal protein L1"
FT                   /id="PRO_0000125657"
SQ   SEQUENCE   229 AA;  24460 MW;  0F2E11FF602C38C2 CRC64;
     MAKKSKKMQE ALKKVDATKA YSVEEAVALA KDTNIAKFDA TVEVAYKLNV DPKKADQQIR
     GAVVLPNGTG KTQTVLVFAK GEKAKEAEAA GADFVGDDDM VAKIQGGWFD FDVVVATPDM
     MATVGKLGRV LGPKGLMPNP KTGTVTMDVT KAVEEVKAGK VTYRVDKAGN IHVPIGKVSF
     DNEKLVENFN TINDVLLKAK PSTAKGQYIK NISVTTTFGP GIHVDQASF
 
 
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