RL5_HALSA
ID RL5_HALSA Reviewed; 175 AA.
AC P50558; P05972; P50556; Q9HPC1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
DE AltName: Full=HCul5;
DE AltName: Full=HHal5;
DE AltName: Full=HL19;
DE AltName: Full=HSal5;
GN Name=rpl5 {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=VNG_1705G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-29.
RX PubMed=152199; DOI=10.1111/j.1432-1033.1978.tb12554.x;
RA Smith N., Matheson A.T., Yaguchi M., Willick G., Nazar R.N.;
RT "The 5-S RNA-protein complex from an extreme halophile, Halobacterium
RT cutirubrum. Purification and characterization.";
RL Eur. J. Biochem. 89:501-509(1978).
RN [3]
RP PROTEIN SEQUENCE OF 2-24.
RC STRAIN=ATCC 33171 / DSM 3754 / JCM 8978 / NCIMB 764 / NRC 34002, and
RC DSM 670;
RX PubMed=8174557; DOI=10.1111/j.1432-1033.1994.tb18791.x;
RA McDougall J., Wittmann-Liebold B.;
RT "Comparative analysis of the protein components from 5S rRNA.protein
RT complexes of halophilic archaebacteria.";
RL Eur. J. Biochem. 221:779-785(1994).
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. May contact 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; contacts the 5S rRNA and
CC probably tRNA. 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; AE004437; AAG19949.1; -; Genomic_DNA.
DR PIR; A84323; A84323.
DR PIR; S08569; S08569.
DR RefSeq; WP_010903247.1; NC_002607.1.
DR AlphaFoldDB; P50558; -.
DR SMR; P50558; -.
DR STRING; 64091.VNG_1705G; -.
DR PaxDb; P50558; -.
DR EnsemblBacteria; AAG19949; AAG19949; VNG_1705G.
DR GeneID; 5954276; -.
DR GeneID; 62887099; -.
DR KEGG; hal:VNG_1705G; -.
DR PATRIC; fig|64091.14.peg.1301; -.
DR HOGENOM; CLU_061015_3_0_2; -.
DR InParanoid; P50558; -.
DR OMA; ERMYAFL; -.
DR OrthoDB; 97230at2157; -.
DR PhylomeDB; P50558; -.
DR Proteomes; UP000000554; 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_A; Ribosomal_L5_A; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR022804; Ribosomal_L5_arc.
DR InterPro; IPR031309; Ribosomal_L5_C.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:152199,
FT ECO:0000269|PubMed:8174557"
FT CHAIN 2..175
FT /note="50S ribosomal protein L5"
FT /id="PRO_0000125053"
SQ SEQUENCE 175 AA; 19507 MW; 8D5B4E7489773BC9 CRC64;
MSETDSTDFH EMREPRIEKV VVHMGVGQGG VELQNAETIL EAITGQQTVR TKAKSPEPEF
GLRQGDPIGA KVTLRDDTAV DFLERALPAA DLDRRQFDNT GNVSFGIEEH TDFPSQEYDP
NIGIYGMDVT VNLTRPGYRV AKRDQGTRQI PSNHRLNSED AVSFLVSNFD VEVNE
