RL2_HALMA
ID RL2_HALMA Reviewed; 240 AA.
AC P20276; Q5V1S7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=50S ribosomal protein L2;
DE AltName: Full=Hl4;
DE AltName: Full=Hmal2;
GN Name=rpl2; OrderedLocusNames=rrnAC1608;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2406244; DOI=10.1016/s0021-9258(19)39729-7;
RA Arndt E., Kroemer W., Hatakeyama T.;
RT "Organization and nucleotide sequence of a gene cluster coding for eight
RT ribosomal proteins in the archaebacterium Halobacterium marismortui.";
RL J. Biol. Chem. 265:3034-3039(1990).
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 REPLACEMENT STUDIES IN E.COLI, AND MUTAGENESIS.
RX PubMed=9531480; DOI=10.1042/bj3310423;
RA Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.;
RT "Functional implications of ribosomal protein L2 in protein biosynthesis as
RT shown by in vivo replacement studies.";
RL Biochem. J. 331:423-430(1998).
RN [4]
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 [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: One of the primary rRNA binding proteins. Required for
CC association of the 30S and 50S subunits to form the 70S ribosome, for
CC tRNA binding and peptide bond formation. It has been suggested to have
CC peptidyltransferase activity; this is somewhat controversial. Makes
CC several contacts with the 16S rRNA in the 70S ribosome (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC subunit in the 70S ribosome (By similarity). Interacts weakly with
CC protein L37Ae. {ECO:0000250, ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128}.
CC -!- MISCELLANEOUS: This protein can be partially incorporated into E.coli
CC polysomes in vivo, indicating it can replace the endogenous protein.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000305}.
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DR EMBL; J05222; AAA86862.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46525.1; -; Genomic_DNA.
DR PIR; F35063; R5HS2L.
DR RefSeq; WP_004957415.1; NZ_CP039138.1.
DR PDB; 1C04; X-ray; 5.00 A; A=46-145.
DR PDB; 1FFK; X-ray; 2.40 A; A=2-240.
DR PDB; 1JJ2; X-ray; 2.40 A; A=2-240.
DR PDB; 1K73; X-ray; 3.01 A; C=2-240.
DR PDB; 1K8A; X-ray; 3.00 A; C=2-240.
DR PDB; 1K9M; X-ray; 3.00 A; C=2-240.
DR PDB; 1KC8; X-ray; 3.01 A; C=2-240.
DR PDB; 1KD1; X-ray; 3.00 A; C=2-240.
DR PDB; 1KQS; X-ray; 3.10 A; A=2-240.
DR PDB; 1M1K; X-ray; 3.20 A; C=2-240.
DR PDB; 1M90; X-ray; 2.80 A; C=2-240.
DR PDB; 1ML5; EM; 14.00 A; d=163-203.
DR PDB; 1N8R; X-ray; 3.00 A; C=2-240.
DR PDB; 1NJI; X-ray; 3.00 A; C=2-240.
DR PDB; 1Q7Y; X-ray; 3.20 A; C=2-240.
DR PDB; 1Q81; X-ray; 2.95 A; C=2-240.
DR PDB; 1Q82; X-ray; 2.98 A; C=2-240.
DR PDB; 1Q86; X-ray; 3.00 A; C=2-240.
DR PDB; 1QVF; X-ray; 3.10 A; A=2-240.
DR PDB; 1QVG; X-ray; 2.90 A; A=2-240.
DR PDB; 1S72; X-ray; 2.40 A; A=1-240.
DR PDB; 1VQ4; X-ray; 2.70 A; A=1-240.
DR PDB; 1VQ5; X-ray; 2.60 A; A=1-240.
DR PDB; 1VQ6; X-ray; 2.70 A; A=1-240.
DR PDB; 1VQ7; X-ray; 2.50 A; A=1-240.
DR PDB; 1VQ8; X-ray; 2.20 A; A=1-240.
DR PDB; 1VQ9; X-ray; 2.40 A; A=1-240.
DR PDB; 1VQK; X-ray; 2.30 A; A=1-240.
DR PDB; 1VQL; X-ray; 2.30 A; A=1-240.
DR PDB; 1VQM; X-ray; 2.30 A; A=1-240.
DR PDB; 1VQN; X-ray; 2.40 A; A=1-240.
DR PDB; 1VQO; X-ray; 2.20 A; A=1-240.
DR PDB; 1VQP; X-ray; 2.25 A; A=1-240.
DR PDB; 1W2B; X-ray; 3.50 A; A=2-240.
DR PDB; 1YHQ; X-ray; 2.40 A; A=1-240.
DR PDB; 1YI2; X-ray; 2.65 A; A=1-240.
DR PDB; 1YIJ; X-ray; 2.60 A; A=1-240.
DR PDB; 1YIT; X-ray; 2.80 A; A=1-240.
DR PDB; 1YJ9; X-ray; 2.90 A; A=1-240.
DR PDB; 1YJN; X-ray; 3.00 A; A=1-240.
DR PDB; 1YJW; X-ray; 2.90 A; A=1-240.
DR PDB; 2OTJ; X-ray; 2.90 A; A=1-240.
DR PDB; 2OTL; X-ray; 2.70 A; A=2-240.
DR PDB; 2QA4; X-ray; 3.00 A; A=1-240.
DR PDB; 2QEX; X-ray; 2.90 A; A=1-240.
DR PDB; 3CC2; X-ray; 2.40 A; A=1-240.
DR PDB; 3CC4; X-ray; 2.70 A; A=1-240.
DR PDB; 3CC7; X-ray; 2.70 A; A=1-240.
DR PDB; 3CCE; X-ray; 2.75 A; A=1-240.
DR PDB; 3CCJ; X-ray; 2.70 A; A=1-240.
DR PDB; 3CCL; X-ray; 2.90 A; A=1-240.
DR PDB; 3CCM; X-ray; 2.55 A; A=1-240.
DR PDB; 3CCQ; X-ray; 2.90 A; A=1-240.
DR PDB; 3CCR; X-ray; 3.00 A; A=1-240.
DR PDB; 3CCS; X-ray; 2.95 A; A=1-240.
DR PDB; 3CCU; X-ray; 2.80 A; A=1-240.
DR PDB; 3CCV; X-ray; 2.90 A; A=1-240.
DR PDB; 3CD6; X-ray; 2.75 A; A=1-240.
DR PDB; 3CMA; X-ray; 2.80 A; A=1-240.
DR PDB; 3CME; X-ray; 2.95 A; A=1-240.
DR PDB; 3CPW; X-ray; 2.70 A; A=1-240.
DR PDB; 3CXC; X-ray; 3.00 A; A=2-240.
DR PDB; 3G4S; X-ray; 3.20 A; A=2-238.
DR PDB; 3G6E; X-ray; 2.70 A; A=2-238.
DR PDB; 3G71; X-ray; 2.85 A; A=2-238.
DR PDB; 3I55; X-ray; 3.11 A; A=1-240.
DR PDB; 3I56; X-ray; 2.90 A; A=1-240.
DR PDB; 3OW2; X-ray; 2.70 A; A=2-238.
DR PDB; 4ADX; EM; 6.60 A; A=1-240.
DR PDB; 4V42; X-ray; 5.50 A; BD=163-203.
DR PDB; 4V9F; X-ray; 2.40 A; A=1-240.
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; 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; 4V9F; -.
DR AlphaFoldDB; P20276; -.
DR SMR; P20276; -.
DR IntAct; P20276; 3.
DR STRING; 272569.rrnAC1608; -.
DR DrugBank; DB04865; Omacetaxine mepesuccinate.
DR EnsemblBacteria; AAV46525; AAV46525; rrnAC1608.
DR GeneID; 40152574; -.
DR GeneID; 64821818; -.
DR KEGG; hma:rrnAC1608; -.
DR PATRIC; fig|272569.17.peg.2298; -.
DR eggNOG; arCOG04067; Archaea.
DR HOGENOM; CLU_036235_0_1_2; -.
DR OMA; SCIELRP; -.
DR EvolutionaryTrace; P20276; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
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; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_A; Ribosomal_L2_A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR023672; Ribosomal_L2_arc.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 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 CHAIN 2..240
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129712"
FT REGION 200..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 200
FT /note="H->A,G: No incorporation into translating E.coli
FT polysomes; ribosomes assemble normally. Significantly
FT reduced translational activity."
FT /evidence="ECO:0000269|PubMed:9531480"
FT CONFLICT 86
FT /note="S -> D (in Ref. 1; AAA86862)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="A -> G (in Ref. 1; AAA86862)"
FT /evidence="ECO:0000305"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1VQ9"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1VQ9"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1YJN"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3CD6"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 161..167
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:3CC4"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 240 AA; 25309 MW; 986CA69D432C7F74 CRC64;
MGRRIQGQRR GRGTSTFRAP SHRYKADLEH RKVEDGDVIA GTVVDIEHDP ARSAPVAAVE
FEDGDRRLIL APEGVGVGDE LQVGVSAEIA PGNTLPLAEI PEGVPVCNVE SSPGDGGKFA
RASGVNAQLL THDRNVAVVK LPSGEMKRLD PQCRATIGVV AGGGRTDKPF VKAGNKHHKM
KARGTKWPNV RGVAMNAVDH PFGGGGRQHP GKPKSISRNA PPGRKVGDIA SKRTGRGGNE
