RL30_HALMA
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 25-MAY-2022, entry version 149.
DE RecName: Full=50S ribosomal protein L30 {ECO:0000255|HAMAP-Rule:MF_01371};
DE AltName: Full=Hl16;
DE AltName: Full=Hl20;
DE AltName: Full=Hmal30;
GN Name=rpl30 {ECO:0000255|HAMAP-Rule:MF_01371}; OrderedLocusNames=rrnAC1591;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2591382; 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 archaebacterium
RT Halobacterium marismortui and their structural relationships to eubacterial
RT and eukaryotic ribosomal proteins.";
RL Eur. J. Biochem. 185:685-693(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1832208; DOI=10.1007/bf00282450;
RA Scholzen T., Arndt E.;
RT "Organization and nucleotide sequence of ten ribosomal protein genes from
RT the region equivalent to the spectinomycin operon in the archaebacterium
RT 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 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [4]
RP PROTEIN SEQUENCE OF 1-30.
RX PubMed=3196689; DOI=10.1021/bi00418a032;
RA Walsh M.J., McDougall J., Wittmann-Liebold B.;
RT "Extended N-terminal sequencing of proteins of archaebacterial ribosomes
RT blotted from two-dimensional gels onto glass fiber and poly(vinylidene
RT 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 / VKM B-1809;
RX 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 / VKM B-1809;
RX 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 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 / VKM B-1809;
RX 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 / VKM B-1809;
RX 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 WITH
RP FOUR MACROLIDE ANTIBIOTICS.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12150912; DOI=10.1016/s1097-2765(02)00570-1;
RA Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.;
RT "The structures of four macrolide antibiotics bound to the large ribosomal
RT 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 / VKM B-1809;
RX 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 WITH
RP FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX 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 center of
RT 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 DIFFERENT
RP 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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RX PubMed=23695244; DOI=10.1107/s0907444913004745;
RA Gabdulkhakov A., Nikonov S., Garber M.;
RT "Revisiting the Haloarcula marismortui 50S ribosomal subunit model.";
RL Acta Crystallogr. D 69:997-1004(2013).
CC -!- FUNCTION: This is one of 5 proteins that mediate the attachment of the
CC 5S rRNA onto the large ribosomal subunit, stabilizing the orientation
CC of adjacent RNA domains.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Binds 5S rRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01371, ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC {ECO:0000255|HAMAP-Rule:MF_01371}.
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DR EMBL; X58395; CAA41292.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46509.1; -; Genomic_DNA.
DR PIR; S16543; R5HS30.
DR RefSeq; WP_004957369.1; NZ_CP039138.1.
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 PDB; 3I55; X-ray; 3.11 A; W=1-154.
DR PDB; 3I56; X-ray; 2.90 A; W=1-154.
DR PDB; 3OW2; X-ray; 2.70 A; V=1-154.
DR PDB; 4ADX; EM; 6.60 A; W=1-154.
DR PDB; 4V9F; X-ray; 2.40 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 PDBsum; 3I55; -.
DR PDBsum; 3I56; -.
DR PDBsum; 3OW2; -.
DR PDBsum; 4ADX; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P14121; -.
DR SMR; P14121; -.
DR IntAct; P14121; 2.
DR STRING; 272569.rrnAC1591; -.
DR EnsemblBacteria; AAV46509; AAV46509; rrnAC1591.
DR GeneID; 40152556; -.
DR GeneID; 64821836; -.
DR KEGG; hma:rrnAC1591; -.
DR PATRIC; fig|272569.17.peg.2280; -.
DR eggNOG; arCOG04086; Archaea.
DR HOGENOM; CLU_055156_6_0_2; -.
DR OMA; KDYITWG; -.
DR EvolutionaryTrace; P14121; -.
DR Proteomes; UP000001169; Chromosome I.
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:UniProtKB-UniRule.
DR CDD; cd01657; Ribosomal_L7_archeal_euk; 1.
DR Gene3D; 3.30.1390.20; -; 1.
DR HAMAP; MF_01371_A; Ribosomal_L30_A; 1.
DR InterPro; IPR036919; L30_ferredoxin-like_sf.
DR InterPro; IPR005997; Ribosomal_L30_arc.
DR InterPro; IPR018038; Ribosomal_L30_CS.
DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR InterPro; IPR035808; Ribosomal_L7_euk_arc.
DR Pfam; PF00327; Ribosomal_L30; 1.
DR SUPFAM; SSF55129; SSF55129; 1.
DR TIGRFAMs; TIGR01309; uL30_arch; 1.
DR PROSITE; PS00634; RIBOSOMAL_L30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..154
FT /note="50S ribosomal protein L30"
FT /id="PRO_0000104622"
FT REGION 114..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 83
FT /note="W -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1VQO"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 154 AA; 17042 MW; ED673F036E974C14 CRC64;
MHALVQLRGE VNMHTDIQDT LEMLNIHHVN HCTLVPETDA YRGMVAKVND FVAFGEPSQE
TLETVLATRA EPLEGDADVD DEWVAEHTDY DDISGLAFAL LSEETTLREQ GLSPTLRLHP
PRGGHDGVKH PVKEGGQLGK HDTEGIDDLL EAMR
