RL5_HALMA
ID RL5_HALMA Reviewed; 177 AA.
AC P14124; Q5V1T6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=50S ribosomal protein L5;
DE AltName: Full=Hl13;
DE AltName: Full=Hmal5;
GN Name=rpl5; OrderedLocusNames=rrnAC1598;
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 2-177.
RX PubMed=2198942; DOI=10.1016/0167-4838(90)90269-l;
RA Hatakeyama T., Hatakeyama T.;
RT "Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the
RT archaebacterium Halobacterium marismortui.";
RL Biochim. Biophys. Acta 1039:343-347(1990).
RN [4]
RP PROTEIN SEQUENCE OF 2-23.
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 11-175 IN 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 1 of 5 proteins that mediates the attachment of the
CC 5S rRNA onto the large ribosomal subunit, stabilizing the orientation
CC of adjacent RNA domains. Forms part of the central protuberance.
CC Modeling places the A and P site tRNAs in close proximity to this
CC protein; the 5S rRNA and some of its associated proteins might help
CC stabilize positioning of ribosome-bound tRNAs. In the 70S ribosome it
CC is thought to contact protein S13 of the 30S subunit (bridge B1b),
CC connecting the 2 subunits; this bridge is implicated in subunit
CC movement.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts with protein L18
CC and the 5S rRNA, and probably with tRNAs. Forms a bridge to the 30S
CC subunit in the 70S ribosome (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
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DR EMBL; X58395; CAA41284.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46516.1; -; Genomic_DNA.
DR PIR; S16535; R5HSL5.
DR RefSeq; WP_004957391.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; D=2-177.
DR PDB; 1JJ2; X-ray; 2.40 A; D=2-177.
DR PDB; 1K73; X-ray; 3.01 A; F=2-177.
DR PDB; 1K8A; X-ray; 3.00 A; F=2-177.
DR PDB; 1K9M; X-ray; 3.00 A; F=2-177.
DR PDB; 1KC8; X-ray; 3.01 A; F=2-177.
DR PDB; 1KD1; X-ray; 3.00 A; F=2-177.
DR PDB; 1KQS; X-ray; 3.10 A; D=2-177.
DR PDB; 1M1K; X-ray; 3.20 A; F=2-177.
DR PDB; 1M90; X-ray; 2.80 A; F=2-177.
DR PDB; 1ML5; EM; 14.00 A; g=2-177.
DR PDB; 1N8R; X-ray; 3.00 A; F=2-177.
DR PDB; 1NJI; X-ray; 3.00 A; F=2-177.
DR PDB; 1Q7Y; X-ray; 3.20 A; F=2-177.
DR PDB; 1Q81; X-ray; 2.95 A; F=2-177.
DR PDB; 1Q82; X-ray; 2.98 A; F=2-177.
DR PDB; 1Q86; X-ray; 3.00 A; F=2-177.
DR PDB; 1QVF; X-ray; 3.10 A; D=2-177.
DR PDB; 1QVG; X-ray; 2.90 A; D=2-177.
DR PDB; 1S72; X-ray; 2.40 A; D=1-177.
DR PDB; 1VQ4; X-ray; 2.70 A; D=1-177.
DR PDB; 1VQ5; X-ray; 2.60 A; D=1-177.
DR PDB; 1VQ6; X-ray; 2.70 A; D=1-177.
DR PDB; 1VQ7; X-ray; 2.50 A; D=1-177.
DR PDB; 1VQ8; X-ray; 2.20 A; D=1-177.
DR PDB; 1VQ9; X-ray; 2.40 A; D=1-177.
DR PDB; 1VQK; X-ray; 2.30 A; D=1-177.
DR PDB; 1VQL; X-ray; 2.30 A; D=1-177.
DR PDB; 1VQM; X-ray; 2.30 A; D=1-177.
DR PDB; 1VQN; X-ray; 2.40 A; D=1-177.
DR PDB; 1VQO; X-ray; 2.20 A; D=1-177.
DR PDB; 1VQP; X-ray; 2.25 A; D=1-177.
DR PDB; 1W2B; X-ray; 3.50 A; D=2-177.
DR PDB; 1YHQ; X-ray; 2.40 A; D=1-177.
DR PDB; 1YI2; X-ray; 2.65 A; D=1-177.
DR PDB; 1YIJ; X-ray; 2.60 A; D=1-177.
DR PDB; 1YIT; X-ray; 2.80 A; D=1-177.
DR PDB; 1YJ9; X-ray; 2.90 A; D=1-177.
DR PDB; 1YJN; X-ray; 3.00 A; D=1-177.
DR PDB; 1YJW; X-ray; 2.90 A; D=1-177.
DR PDB; 2OTJ; X-ray; 2.90 A; D=1-177.
DR PDB; 2OTL; X-ray; 2.70 A; D=1-177.
DR PDB; 2QA4; X-ray; 3.00 A; D=1-177.
DR PDB; 2QEX; X-ray; 2.90 A; D=1-177.
DR PDB; 3CC2; X-ray; 2.40 A; D=1-177.
DR PDB; 3CC4; X-ray; 2.70 A; D=1-177.
DR PDB; 3CC7; X-ray; 2.70 A; D=1-177.
DR PDB; 3CCE; X-ray; 2.75 A; D=1-177.
DR PDB; 3CCJ; X-ray; 2.70 A; D=1-177.
DR PDB; 3CCL; X-ray; 2.90 A; D=1-177.
DR PDB; 3CCM; X-ray; 2.55 A; D=1-177.
DR PDB; 3CCQ; X-ray; 2.90 A; D=1-177.
DR PDB; 3CCR; X-ray; 3.00 A; D=1-177.
DR PDB; 3CCS; X-ray; 2.95 A; D=1-177.
DR PDB; 3CCU; X-ray; 2.80 A; D=1-177.
DR PDB; 3CCV; X-ray; 2.90 A; D=1-177.
DR PDB; 3CD6; X-ray; 2.75 A; D=1-177.
DR PDB; 3CMA; X-ray; 2.80 A; D=1-177.
DR PDB; 3CME; X-ray; 2.95 A; D=1-177.
DR PDB; 3CPW; X-ray; 2.70 A; D=1-177.
DR PDB; 3CXC; X-ray; 3.00 A; D=2-177.
DR PDB; 3G4S; X-ray; 3.20 A; D=1-177.
DR PDB; 3G6E; X-ray; 2.70 A; D=1-177.
DR PDB; 3G71; X-ray; 2.85 A; D=1-177.
DR PDB; 3I55; X-ray; 3.11 A; D=1-177.
DR PDB; 3I56; X-ray; 2.90 A; D=1-177.
DR PDB; 3OW2; X-ray; 2.70 A; D=11-175.
DR PDB; 4ADX; EM; 6.60 A; D=1-177.
DR PDB; 4V42; X-ray; 5.50 A; BG=2-177.
DR PDB; 4V4R; X-ray; 5.90 A; BG=2-177.
DR PDB; 4V4S; X-ray; 6.76 A; G=2-177.
DR PDB; 4V4T; X-ray; 6.46 A; G=2-177.
DR PDB; 4V9F; X-ray; 2.40 A; D=1-177.
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; 1ML5; -.
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; 4V42; -.
DR PDBsum; 4V4R; -.
DR PDBsum; 4V4S; -.
DR PDBsum; 4V4T; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P14124; -.
DR SMR; P14124; -.
DR IntAct; P14124; 3.
DR STRING; 272569.rrnAC1598; -.
DR EnsemblBacteria; AAV46516; AAV46516; rrnAC1598.
DR GeneID; 40152564; -.
DR GeneID; 64821828; -.
DR KEGG; hma:rrnAC1598; -.
DR PATRIC; fig|272569.17.peg.2288; -.
DR eggNOG; arCOG04092; Archaea.
DR HOGENOM; CLU_061015_3_0_2; -.
DR OMA; ERMYAFL; -.
DR EvolutionaryTrace; P14124; -.
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: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; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2198942,
FT ECO:0000269|PubMed:3196689"
FT CHAIN 2..177
FT /note="50S ribosomal protein L5"
FT /id="PRO_0000125051"
FT CONFLICT 134
FT /note="N -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3G6E"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1VQ6"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 177 AA; 19528 MW; 565902FAA3D95FB6 CRC64;
MSSESESGGD FHEMREPRIE KVVVHMGIGH GGRDLANAED ILGEITGQMP VRTKAKRTVG
EFDIREGDPI GAKVTLRDEM AEEFLQTALP LAELATSQFD DTGNFSFGVE EHTEFPSQEY
DPSIGIYGLD VTVNLVRPGY RVAKRDKASR SIPTKHRLNP ADAVAFIEST YDVEVSE
