RL6_HALMA
ID RL6_HALMA Reviewed; 178 AA.
AC P14135; P12739; Q5V1T8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
DE AltName: Full=Hl10;
DE AltName: Full=Hmal6;
GN Name=rpl6 {ECO:0000255|HAMAP-Rule:MF_01365}; OrderedLocusNames=rrnAC1596;
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 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 [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-55.
RX PubMed=3311072; DOI=10.1515/bchm3.1987.368.2.921;
RA Dijk J., van den Broek R., Nasiulas G., Beck A., Reinhardt R.,
RA Wittmann-Liebold B.;
RT "The N-terminal sequence of ribosomal protein L10 from the archaebacterium
RT Halobacterium marismortui and its relationship to eubacterial protein L6
RT and other ribosomal proteins.";
RL Biol. Chem. Hoppe-Seyler 368:921-925(1987).
RN [4]
RP PROTEIN SEQUENCE OF 2-31.
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 3D-STRUCTURE MODELING.
RX PubMed=10476961; DOI=10.1038/23641;
RA Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A.;
RT "Placement of protein and RNA structures into a 5 A-resolution map of the
RT 50S ribosomal subunit.";
RL Nature 400:841-847(1999).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 protein binds to the 23S rRNA, and is important in its
CC secondary structure. It is located near the subunit interface in the
CC base of the L7/L12 stalk, and near the tRNA binding site of the
CC peptidyltransferase center.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts weakly with
CC protein L13. {ECO:0000255|HAMAP-Rule:MF_01365,
CC ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC {ECO:0000255|HAMAP-Rule:MF_01365}.
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; CAA41287.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46514.1; -; Genomic_DNA.
DR PIR; S16538; R5HS6L.
DR RefSeq; WP_011223740.1; NZ_CP039138.1.
DR PDB; 1C04; X-ray; 5.00 A; B=21-25.
DR PDB; 1FFK; X-ray; 2.40 A; 1=2-178.
DR PDB; 1JJ2; X-ray; 2.40 A; E=2-178.
DR PDB; 1K73; X-ray; 3.01 A; G=2-178.
DR PDB; 1K8A; X-ray; 3.00 A; G=2-178.
DR PDB; 1K9M; X-ray; 3.00 A; G=2-178.
DR PDB; 1KC8; X-ray; 3.01 A; G=2-178.
DR PDB; 1KD1; X-ray; 3.00 A; G=2-178.
DR PDB; 1KQS; X-ray; 3.10 A; E=2-178.
DR PDB; 1M1K; X-ray; 3.20 A; G=2-178.
DR PDB; 1M90; X-ray; 2.80 A; G=2-178.
DR PDB; 1N8R; X-ray; 3.00 A; G=2-178.
DR PDB; 1NJI; X-ray; 3.00 A; G=2-178.
DR PDB; 1Q7Y; X-ray; 3.20 A; G=2-178.
DR PDB; 1Q81; X-ray; 2.95 A; G=2-178.
DR PDB; 1Q82; X-ray; 2.98 A; G=2-178.
DR PDB; 1Q86; X-ray; 3.00 A; G=2-178.
DR PDB; 1QVF; X-ray; 3.10 A; E=2-178.
DR PDB; 1QVG; X-ray; 2.90 A; E=2-178.
DR PDB; 1S72; X-ray; 2.40 A; E=1-178.
DR PDB; 1VQ4; X-ray; 2.70 A; E=1-178.
DR PDB; 1VQ5; X-ray; 2.60 A; E=1-178.
DR PDB; 1VQ6; X-ray; 2.70 A; E=1-178.
DR PDB; 1VQ7; X-ray; 2.50 A; E=1-178.
DR PDB; 1VQ8; X-ray; 2.20 A; E=1-178.
DR PDB; 1VQ9; X-ray; 2.40 A; E=1-178.
DR PDB; 1VQK; X-ray; 2.30 A; E=1-178.
DR PDB; 1VQL; X-ray; 2.30 A; E=1-178.
DR PDB; 1VQM; X-ray; 2.30 A; E=1-178.
DR PDB; 1VQN; X-ray; 2.40 A; E=1-178.
DR PDB; 1VQO; X-ray; 2.20 A; E=1-178.
DR PDB; 1VQP; X-ray; 2.25 A; E=1-178.
DR PDB; 1W2B; X-ray; 3.50 A; E=2-178.
DR PDB; 1YHQ; X-ray; 2.40 A; E=1-178.
DR PDB; 1YI2; X-ray; 2.65 A; E=1-178.
DR PDB; 1YIJ; X-ray; 2.60 A; E=1-178.
DR PDB; 1YIT; X-ray; 2.80 A; E=1-178.
DR PDB; 1YJ9; X-ray; 2.90 A; E=1-178.
DR PDB; 1YJN; X-ray; 3.00 A; E=1-178.
DR PDB; 1YJW; X-ray; 2.90 A; E=1-178.
DR PDB; 2OTJ; X-ray; 2.90 A; E=1-178.
DR PDB; 2OTL; X-ray; 2.70 A; E=1-178.
DR PDB; 2QA4; X-ray; 3.00 A; E=1-178.
DR PDB; 2QEX; X-ray; 2.90 A; E=1-178.
DR PDB; 3CC2; X-ray; 2.40 A; E=1-178.
DR PDB; 3CC4; X-ray; 2.70 A; E=1-178.
DR PDB; 3CC7; X-ray; 2.70 A; E=1-178.
DR PDB; 3CCE; X-ray; 2.75 A; E=1-178.
DR PDB; 3CCJ; X-ray; 2.70 A; E=1-178.
DR PDB; 3CCL; X-ray; 2.90 A; E=1-178.
DR PDB; 3CCM; X-ray; 2.55 A; E=1-178.
DR PDB; 3CCQ; X-ray; 2.90 A; E=1-178.
DR PDB; 3CCR; X-ray; 3.00 A; E=1-178.
DR PDB; 3CCS; X-ray; 2.95 A; E=1-178.
DR PDB; 3CCU; X-ray; 2.80 A; E=1-178.
DR PDB; 3CCV; X-ray; 2.90 A; E=1-178.
DR PDB; 3CD6; X-ray; 2.75 A; E=1-178.
DR PDB; 3CMA; X-ray; 2.80 A; E=1-178.
DR PDB; 3CME; X-ray; 2.95 A; E=1-178.
DR PDB; 3CPW; X-ray; 2.70 A; E=1-178.
DR PDB; 3CXC; X-ray; 3.00 A; E=2-178.
DR PDB; 3G4S; X-ray; 3.20 A; E=2-173.
DR PDB; 3G6E; X-ray; 2.70 A; E=2-173.
DR PDB; 3G71; X-ray; 2.85 A; E=2-173.
DR PDB; 3I55; X-ray; 3.11 A; E=1-178.
DR PDB; 3I56; X-ray; 2.90 A; E=1-178.
DR PDB; 3OW2; X-ray; 2.70 A; E=2-173.
DR PDB; 4ADX; EM; 6.60 A; E=1-178.
DR PDB; 4V9F; X-ray; 2.40 A; E=1-178.
DR PDBsum; 1C04; -.
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; P14135; -.
DR SMR; P14135; -.
DR IntAct; P14135; 2.
DR STRING; 272569.rrnAC1596; -.
DR EnsemblBacteria; AAV46514; AAV46514; rrnAC1596.
DR GeneID; 40152561; -.
DR KEGG; hma:rrnAC1596; -.
DR PATRIC; fig|272569.17.peg.2285; -.
DR eggNOG; arCOG04090; Archaea.
DR HOGENOM; CLU_065464_0_0_2; -.
DR OMA; VFQDGIY; -.
DR EvolutionaryTrace; P14135; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.930.12; -; 2.
DR HAMAP; MF_01365_A; Ribosomal_L6_A; 1.
DR InterPro; IPR000702; Ribosomal_L6.
DR InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR InterPro; IPR002359; Ribosomal_L6_CS2.
DR InterPro; IPR019907; Ribosomal_L6P_arc.
DR PANTHER; PTHR11655; PTHR11655; 1.
DR Pfam; PF00347; Ribosomal_L6; 2.
DR PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR SUPFAM; SSF56053; SSF56053; 2.
DR TIGRFAMs; TIGR03653; uL6_arch; 1.
DR PROSITE; PS00700; RIBOSOMAL_L6_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3196689,
FT ECO:0000269|PubMed:3311072"
FT CHAIN 2..178
FT /note="50S ribosomal protein L6"
FT /id="PRO_0000131083"
FT VARIANT 3
FT /note="R -> S"
FT VARIANT 24
FT /note="E -> S"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 57..77
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 178 AA; 19944 MW; 380872452165689C CRC64;
MPRVELEIPE DVDAEQDHLD ITVEGDNGSV TRRLWYPDID VSVDGDTVVI ESDEDNAKTM
STIGTFQSHI ENMFHGVTEG WEYGMEVFYS HFPMQVNVEG DEVVIENFLG EKAPRRTTIH
GDTDVEIDGE ELTVSGPDIE AVGQTAADIE QLTRINDKDV RVFQDGVYIT RKPNRGDA
