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RL5_THEMA
ID   RL5_THEMA               Reviewed;         184 AA.
AC   P38517;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=TM_1488;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=8002596; DOI=10.1128/jb.176.24.7703-7710.1994;
RA   Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.;
RT   "Phylogenetic depth of S10 and spc operons: cloning and sequencing of a
RT   ribosomal protein gene cluster from the extremely thermophilic bacterium
RT   Thermotoga maritima.";
RL   J. Bacteriol. 176:7703-7710(1994).
RN   [2]
RP   SEQUENCE REVISION TO 158.
RA   Sanangelantoni A.M.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: This is 1 of the proteins that binds and probably mediates
CC       the attachment of the 5S RNA into the large ribosomal subunit, where it
CC       forms part of the central protuberance. In the 70S ribosome it contacts
CC       protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits;
CC       this bridge is implicated in subunit movement. Contacts the P site
CC       tRNA; the 5S rRNA and some of its associated proteins might help
CC       stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_01333}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC       rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA.
CC       Forms a bridge to the 30S subunit in the 70S ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01333}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01333}.
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DR   EMBL; Z21677; CAA79789.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD36554.1; -; Genomic_DNA.
DR   PIR; H72248; H72248.
DR   RefSeq; NP_229288.1; NC_000853.1.
DR   RefSeq; WP_004081811.1; NZ_CP011107.1.
DR   AlphaFoldDB; P38517; -.
DR   SMR; P38517; -.
DR   STRING; 243274.THEMA_06860; -.
DR   EnsemblBacteria; AAD36554; AAD36554; TM_1488.
DR   KEGG; tma:TM1488; -.
DR   eggNOG; COG0094; Bacteria.
DR   InParanoid; P38517; -.
DR   OMA; ERMYAFL; -.
DR   OrthoDB; 1456375at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1440.10; -; 1.
DR   HAMAP; MF_01333_B; Ribosomal_L5_B; 1.
DR   InterPro; IPR002132; Ribosomal_L5.
DR   InterPro; IPR020930; Ribosomal_L5_bac-type.
DR   InterPro; IPR031309; Ribosomal_L5_C.
DR   InterPro; IPR020929; Ribosomal_L5_CS.
DR   InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR   InterPro; IPR031310; Ribosomal_L5_N.
DR   PANTHER; PTHR11994; PTHR11994; 1.
DR   Pfam; PF00281; Ribosomal_L5; 1.
DR   Pfam; PF00673; Ribosomal_L5_C; 1.
DR   PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR   SUPFAM; SSF55282; SSF55282; 1.
DR   PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..184
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000125012"
FT   CONFLICT        24
FT                   /note="F -> L (in Ref. 1; CAA79789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="N -> S (in Ref. 1; CAA79789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="N -> D (in Ref. 1; CAA79789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="A -> V (in Ref. 1; CAA79789)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   184 AA;  21306 MW;  52702CB5A4513989 CRC64;
     MRYEYVPLKD QYEKEIVPAL MKEFNYKNIH QVPKLVKIVI NMGIGEGSRN YDLIERHANE
     LAKITGQKPI VTRARKSISN FKIRKGMPIG LKVTLRGARM YNFLYKLINI VLPKVRDFRG
     LDPNSFDGRG NYSFGLSEQL VFPELNPDEV RRIQGMDITI VTTAKTDQEA RRLLELFGMP
     FKRG
 
 
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