ID RL30_HALMA Reviewed; 154 AA. AC P14121; Q5V1U3; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 2. DT 19-JAN-2010, entry version 86. DE RecName: Full=50S ribosomal protein L30P; DE AltName: Full=Hmal30; DE AltName: Full=Hl20; DE AltName: Full=Hl16; GN Name=rpl30p; OrderedLocusNames=rrnAC1591; OS Haloarcula marismortui (Halobacterium marismortui). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloarcula. OX NCBI_TaxID=2238; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=90076190; PubMed=2591382; RX DOI=10.1111/j.1432-1033.1989.tb15166.x; RA Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T.; RT "Primary structures of five ribosomal proteins from the RT archaebacterium Halobacterium marismortui and their structural RT relationships to eubacterial and eukaryotic ribosomal proteins."; RL Eur. J. Biochem. 185:685-693(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91360093; PubMed=1832208; DOI=10.1007/BF00282450; RA Scholzen T., Arndt E.; RT "Organization and nucleotide sequence of ten ribosomal protein genes RT from the region equivalent to the spectinomycin operon in the RT archaebacterium Halobacterium marismortui."; RL Mol. Gen. Genet. 228:70-80(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966; RX PubMed=15520287; DOI=10.1101/gr.2700304; RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., RA Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., RA Date S.V., Marcotte E., Hood L., Ng W.V.; RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from RT the Dead Sea."; RL Genome Res. 14:2221-2234(2004). RN [4] RP PROTEIN SEQUENCE OF 1-30. RX MEDLINE=89062418; PubMed=3196689; DOI=10.1021/bi00418a032; RA Walsh M.J., McDougall J., Wittmann-Liebold B.; RT "Extended N-terminal sequencing of proteins of archaebacterial RT ribosomes blotted from two-dimensional gels onto glass fiber and RT poly(vinylidene difluoride) membrane."; RL Biochemistry 27:6867-6876(1988). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966; RX MEDLINE=20396344; PubMed=10937989; DOI=10.1126/science.289.5481.905; RA Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.; RT "The complete atomic structure of the large ribosomal subunit at 2.4 A RT resolution."; RL Science 289:905-920(2000). RN [6] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966; RX MEDLINE=20396345; PubMed=10937990; DOI=10.1126/science.289.5481.920; RA Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.; RT "The structural basis of ribosome activity in peptide bond RT synthesis."; RL Science 289:920-930(2000). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966; RX MEDLINE=21864647; PubMed=11828326; DOI=10.1038/nsb758; RA Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K., RA Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.; RT "A pre-translocational intermediate in protein synthesis observed in RT crystals of enzymatically active 50S subunits."; RL Nat. Struct. Biol. 9:225-230(2002). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966; RX MEDLINE=21376068; PubMed=11483524; DOI=10.1093/emboj/20.15.4214; RA Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.; RT "The kink-turn: a new RNA secondary structure motif."; RL EMBO J. 20:4214-4221(2001). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX RP WITH FOUR MACROLIDE ANTIBIOTICS. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966; RX MEDLINE=22146556; PubMed=12150912; DOI=10.1016/S1097-2765(02)00570-1; RA Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., RA Steitz T.A.; RT "The structures of four macrolide antibiotics bound to the large RT ribosomal subunit."; RL Mol. Cell 10:117-128(2002). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966; RX MEDLINE=22199842; PubMed=12185246; DOI=10.1073/pnas.172404099; RA Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.; RT "Structural insights into peptide bond formation."; RL Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002). RN [11] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX RP WITH FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966; RX MEDLINE=22745177; PubMed=12860128; DOI=10.1016/S0022-2836(03)00668-5; RA Hansen J.L., Moore P.B., Steitz T.A.; RT "Structures of five antibiotics bound at the peptidyl transferase RT center of the large ribosomal subunit."; RL J. Mol. Biol. 330:1061-1075(2003). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO RP DIFFERENT E SITE SUBSTRATES. RX PubMed=14561884; DOI=10.1261/rna.5120503; RA Schmeing T.M., Moore P.B., Steitz T.A.; RT "Structures of deacylated tRNA mimics bound to the E site of the large RT ribosomal subunit."; RL RNA 9:1345-1352(2003). CC -!- FUNCTION: This is one of 5 proteins that mediate the attachment of CC the 5S rRNA onto the large ribosomal subunit, stabilizing the CC orientation of adjacent RNA domains. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Binds 5S rRNA. CC -!- SIMILARITY: Belongs to the ribosomal protein L30P family. 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; X58395; CAA41292.1; -; Genomic_DNA. DR EMBL; AY596297; AAV46509.1; -; Genomic_DNA. DR PIR; S16543; R5HS30. DR RefSeq; YP_136215.1; -. DR PDB; 1FFK; X-ray; 2.40 A; T=1-154. DR PDB; 1JJ2; X-ray; 2.40 A; V=1-154. DR PDB; 1K73; X-ray; 3.01 A; X=1-154. DR PDB; 1K8A; X-ray; 3.00 A; X=1-154. DR PDB; 1K9M; X-ray; 3.00 A; X=1-154. DR PDB; 1KC8; X-ray; 3.01 A; X=1-154. DR PDB; 1KD1; X-ray; 3.00 A; X=1-154. DR PDB; 1KQS; X-ray; 3.10 A; V=1-154. DR PDB; 1M1K; X-ray; 3.20 A; X=1-154. DR PDB; 1M90; X-ray; 2.80 A; X=1-154. DR PDB; 1N8R; X-ray; 3.00 A; X=1-154. DR PDB; 1NJI; X-ray; 3.00 A; X=1-154. DR PDB; 1Q7Y; X-ray; 3.20 A; X=1-154. DR PDB; 1Q81; X-ray; 2.95 A; X=1-154. DR PDB; 1Q82; X-ray; 2.98 A; X=1-154. DR PDB; 1Q86; X-ray; 3.00 A; X=1-154. DR PDB; 1QVF; X-ray; 3.10 A; V=1-154. DR PDB; 1QVG; X-ray; 2.90 A; V=1-154. DR PDB; 1S72; X-ray; 2.40 A; W=1-154. DR PDB; 1VQ4; X-ray; 2.70 A; W=1-154. DR PDB; 1VQ5; X-ray; 2.60 A; W=1-154. DR PDB; 1VQ6; X-ray; 2.70 A; W=1-154. DR PDB; 1VQ7; X-ray; 2.50 A; W=1-154. DR PDB; 1VQ8; X-ray; 2.20 A; W=1-154. DR PDB; 1VQ9; X-ray; 2.40 A; W=1-154. DR PDB; 1VQK; X-ray; 2.30 A; W=1-154. DR PDB; 1VQL; X-ray; 2.30 A; W=1-154. DR PDB; 1VQM; X-ray; 2.30 A; W=1-154. DR PDB; 1VQN; X-ray; 2.40 A; W=1-154. DR PDB; 1VQO; X-ray; 2.20 A; W=1-154. DR PDB; 1VQP; X-ray; 2.25 A; W=1-154. DR PDB; 1W2B; X-ray; 3.50 A; V=1-154. DR PDB; 1YHQ; X-ray; 2.40 A; W=1-154. DR PDB; 1YI2; X-ray; 2.65 A; W=1-154. DR PDB; 1YIJ; X-ray; 2.60 A; W=1-154. DR PDB; 1YIT; X-ray; 2.80 A; W=1-154. DR PDB; 1YJ9; X-ray; 2.90 A; W=1-154. DR PDB; 1YJN; X-ray; 3.00 A; W=1-154. DR PDB; 1YJW; X-ray; 2.90 A; W=1-154. DR PDB; 2OTJ; X-ray; 2.90 A; W=1-154. DR PDB; 2OTL; X-ray; 2.70 A; W=1-154. DR PDB; 2QA4; X-ray; 3.00 A; W=1-154. DR PDB; 2QEX; X-ray; 2.90 A; W=1-154. DR PDB; 3CC2; X-ray; 2.40 A; W=1-154. DR PDB; 3CC4; X-ray; 2.70 A; W=1-154. DR PDB; 3CC7; X-ray; 2.70 A; W=1-154. DR PDB; 3CCE; X-ray; 2.75 A; W=1-154. DR PDB; 3CCJ; X-ray; 2.70 A; W=1-154. DR PDB; 3CCL; X-ray; 2.90 A; W=1-154. DR PDB; 3CCM; X-ray; 2.55 A; W=1-154. DR PDB; 3CCQ; X-ray; 2.90 A; W=1-154. DR PDB; 3CCR; X-ray; 3.00 A; W=1-154. DR PDB; 3CCS; X-ray; 2.95 A; W=1-154. DR PDB; 3CCU; X-ray; 2.80 A; W=1-154. DR PDB; 3CCV; X-ray; 2.90 A; W=1-154. DR PDB; 3CD6; X-ray; 2.75 A; W=1-154. DR PDB; 3CMA; X-ray; 2.80 A; W=1-154. DR PDB; 3CME; X-ray; 2.95 A; W=1-154. DR PDB; 3CPW; X-ray; 2.70 A; V=1-154. DR PDB; 3CXC; X-ray; 3.00 A; V=1-154. DR PDB; 3G4S; X-ray; 3.20 A; W=1-154. DR PDB; 3G6E; X-ray; 2.70 A; W=1-154. DR PDB; 3G71; X-ray; 2.85 A; W=1-154. DR PDBsum; 1FFK; -. DR PDBsum; 1JJ2; -. DR PDBsum; 1K73; -. DR PDBsum; 1K8A; -. DR PDBsum; 1K9M; -. DR PDBsum; 1KC8; -. DR PDBsum; 1KD1; -. DR PDBsum; 1KQS; -. DR PDBsum; 1M1K; -. DR PDBsum; 1M90; -. DR PDBsum; 1N8R; -. DR PDBsum; 1NJI; -. DR PDBsum; 1Q7Y; -. DR PDBsum; 1Q81; -. DR PDBsum; 1Q82; -. DR PDBsum; 1Q86; -. DR PDBsum; 1QVF; -. DR PDBsum; 1QVG; -. DR PDBsum; 1S72; -. DR PDBsum; 1VQ4; -. DR PDBsum; 1VQ5; -. DR PDBsum; 1VQ6; -. DR PDBsum; 1VQ7; -. DR PDBsum; 1VQ8; -. DR PDBsum; 1VQ9; -. DR PDBsum; 1VQK; -. DR PDBsum; 1VQL; -. DR PDBsum; 1VQM; -. DR PDBsum; 1VQN; -. DR PDBsum; 1VQO; -. DR PDBsum; 1VQP; -. DR PDBsum; 1W2B; -. DR PDBsum; 1YHQ; -. DR PDBsum; 1YI2; -. DR PDBsum; 1YIJ; -. DR PDBsum; 1YIT; -. DR PDBsum; 1YJ9; -. DR PDBsum; 1YJN; -. DR PDBsum; 1YJW; -. DR PDBsum; 2OTJ; -. DR PDBsum; 2OTL; -. DR PDBsum; 2QA4; -. DR PDBsum; 2QEX; -. DR PDBsum; 3CC2; -. DR PDBsum; 3CC4; -. DR PDBsum; 3CC7; -. DR PDBsum; 3CCE; -. DR PDBsum; 3CCJ; -. DR PDBsum; 3CCL; -. DR PDBsum; 3CCM; -. DR PDBsum; 3CCQ; -. DR PDBsum; 3CCR; -. DR PDBsum; 3CCS; -. DR PDBsum; 3CCU; -. DR PDBsum; 3CCV; -. DR PDBsum; 3CD6; -. DR PDBsum; 3CMA; -. DR PDBsum; 3CME; -. DR PDBsum; 3CPW; -. DR PDBsum; 3CXC; -. DR PDBsum; 3G4S; -. DR PDBsum; 3G6E; -. DR PDBsum; 3G71; -. DR GeneID; 3127531; -. DR GenomeReviews; AY596297_GR; rrnAC1591. DR KEGG; hma:rrnAC1591; -. DR NMPDR; fig|272569.1.peg.1482; -. DR HOGENOM; HBG297538; -. DR OMA; HPPRKGH; -. DR BioCyc; HMAR272569:RRNAC1591-MONOMER; -. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:HAMAP. DR HAMAP; MF_01371_A; Ribosomal_L30_A; 1; -. DR InterPro; IPR005997; Ribosomal_L30_arc. DR InterPro; IPR018038; Ribosomal_L30_CS. DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like. DR InterPro; IPR000517; Ribosomal_L30p/L7e_cons-reg. DR Pfam; PF00327; Ribosomal_L30; 1. DR PROSITE; PS00634; RIBOSOMAL_L30; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 154 50S ribosomal protein L30P. FT /FTId=PRO_0000104622. FT CONFLICT 83 83 W -> L (in Ref. 2). FT CONFLICT 148 148 Missing (in Ref. 2). FT STRAND 2 6 FT HELIX 15 23 FT STRAND 31 35 FT HELIX 39 48 FT HELIX 49 51 FT STRAND 52 55 FT HELIX 59 69 FT STRAND 72 76 FT HELIX 81 87 FT STRAND 88 92 FT HELIX 93 101 FT TURN 107 111 FT STRAND 128 131 FT HELIX 132 134 FT STRAND 136 140 FT HELIX 143 152 SQ SEQUENCE 154 AA; 17042 MW; ED673F036E974C14 CRC64; MHALVQLRGE VNMHTDIQDT LEMLNIHHVN HCTLVPETDA YRGMVAKVND FVAFGEPSQE TLETVLATRA EPLEGDADVD DEWVAEHTDY DDISGLAFAL LSEETTLREQ GLSPTLRLHP PRGGHDGVKH PVKEGGQLGK HDTEGIDDLL EAMR //