RL10_HALMA
ID RL10_HALMA Reviewed; 348 AA.
AC P15825; Q5V2A8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00280};
DE AltName: Full=Acidic ribosomal protein P0 homolog {ECO:0000255|HAMAP-Rule:MF_00280};
DE AltName: Full=HMal10;
DE AltName: Full=L10E;
GN Name=rpl10 {ECO:0000255|HAMAP-Rule:MF_00280};
GN Synonyms=rpl10e, rplP0 {ECO:0000255|HAMAP-Rule:MF_00280};
GN OrderedLocusNames=rrnAC1417;
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=2320419; DOI=10.1093/nar/18.5.1285;
RA Arndt E., Weigel C.;
RT "Nucleotide sequence of the genes encoding the L11, L1, L10 and L12
RT equivalent ribosomal proteins from the archaebacterium Halobacterium
RT marismortui.";
RL Nucleic Acids Res. 18:1285-1285(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 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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP MODEL, AND PROBABLE INTERACTION WITH L11 (RPL11) AND L12 (RPL12).
RX PubMed=15989950; DOI=10.1016/j.cell.2005.04.015;
RA Diaconu M., Kothe U., Schlunzen F., Fischer N., Harms J.M.,
RA Tonevitsky A.G., Stark H., Rodnina M.V., Wahl M.C.;
RT "Structural basis for the function of the ribosomal L7/12 stalk in factor
RT binding and GTPase activation.";
RL Cell 121:991-1004(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), RRNA-BINDING, AND INTERACTION WITH
RP L11.
RX PubMed=17599351; DOI=10.1016/j.jmb.2007.05.091;
RA Kavran J.M., Steitz T.A.;
RT "Structure of the base of the L7/L12 stalk of the Haloarcula marismortui
RT large ribosomal subunit: analysis of L11 movements.";
RL J. Mol. Biol. 371:1047-1059(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 6-211 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: Forms part of the ribosomal stalk, playing a central role in
CC the interaction of the ribosome with GTP-bound translation factors.
CC {ECO:0000305}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms part of the ribosomal
CC stalk which helps the ribosome interact with GTP-bound translation
CC factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10
CC forms an elongated spine to which the L12 dimers bind in a sequential
CC fashion (Probable). {ECO:0000305|PubMed:12150912,
CC ECO:0000305|PubMed:12860128}.
CC -!- MISCELLANEOUS: Has been called L10e and L10E in this organism; in this
CC case 'e/E' is for E.coli-like, not eukaryotic-type protein.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000255|HAMAP-Rule:MF_00280}.
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DR EMBL; X51430; CAA35795.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46344.1; -; Genomic_DNA.
DR PIR; S08422; R5HS10.
DR RefSeq; WP_011223609.1; NZ_CP039138.1.
DR PDB; 1JJ2; X-ray; 2.40 A; G=1-348.
DR PDB; 1K73; X-ray; 3.01 A; I=1-348.
DR PDB; 1K8A; X-ray; 3.00 A; I=1-348.
DR PDB; 1K9M; X-ray; 3.00 A; I=1-348.
DR PDB; 1KC8; X-ray; 3.01 A; I=1-348.
DR PDB; 1KD1; X-ray; 3.00 A; I=1-348.
DR PDB; 1KQS; X-ray; 3.10 A; G=1-348.
DR PDB; 1M1K; X-ray; 3.20 A; I=1-348.
DR PDB; 1M90; X-ray; 2.80 A; I=1-348.
DR PDB; 1N8R; X-ray; 3.00 A; I=1-348.
DR PDB; 1NJI; X-ray; 3.00 A; I=1-348.
DR PDB; 1Q7Y; X-ray; 3.20 A; I=1-348.
DR PDB; 1Q81; X-ray; 2.95 A; I=1-348.
DR PDB; 1Q82; X-ray; 2.98 A; I=1-348.
DR PDB; 1Q86; X-ray; 3.00 A; I=1-348.
DR PDB; 1QVF; X-ray; 3.10 A; G=1-348.
DR PDB; 1QVG; X-ray; 2.90 A; G=1-348.
DR PDB; 1S72; X-ray; 2.40 A; G=1-348.
DR PDB; 1VQ4; X-ray; 2.70 A; G=1-348.
DR PDB; 1VQ5; X-ray; 2.60 A; G=1-348.
DR PDB; 1VQ6; X-ray; 2.70 A; G=1-348.
DR PDB; 1VQ7; X-ray; 2.50 A; G=1-348.
DR PDB; 1VQ8; X-ray; 2.20 A; G=1-348.
DR PDB; 1VQ9; X-ray; 2.40 A; G=1-348.
DR PDB; 1VQK; X-ray; 2.30 A; G=1-348.
DR PDB; 1VQL; X-ray; 2.30 A; G=1-348.
DR PDB; 1VQM; X-ray; 2.30 A; G=1-348.
DR PDB; 1VQN; X-ray; 2.40 A; G=1-348.
DR PDB; 1VQO; X-ray; 2.20 A; G=1-348.
DR PDB; 1VQP; X-ray; 2.25 A; G=1-348.
DR PDB; 1W2B; X-ray; 3.50 A; G=1-348.
DR PDB; 1YHQ; X-ray; 2.40 A; G=1-348.
DR PDB; 1YI2; X-ray; 2.65 A; G=1-348.
DR PDB; 1YIJ; X-ray; 2.60 A; G=1-348.
DR PDB; 1YIT; X-ray; 2.80 A; G=1-348.
DR PDB; 1YJ9; X-ray; 2.90 A; G=1-348.
DR PDB; 1YJN; X-ray; 3.00 A; G=1-348.
DR PDB; 1YJW; X-ray; 2.90 A; G=1-348.
DR PDB; 2OTJ; X-ray; 2.90 A; G=1-348.
DR PDB; 2OTL; X-ray; 2.70 A; G=1-348.
DR PDB; 2QA4; X-ray; 3.00 A; G=1-348.
DR PDB; 2QEX; X-ray; 2.90 A; G=1-348.
DR PDB; 3CC2; X-ray; 2.40 A; G=1-348.
DR PDB; 3CC4; X-ray; 2.70 A; G=1-348.
DR PDB; 3CC7; X-ray; 2.70 A; G=1-348.
DR PDB; 3CCE; X-ray; 2.75 A; G=1-348.
DR PDB; 3CCJ; X-ray; 2.70 A; G=1-348.
DR PDB; 3CCL; X-ray; 2.90 A; G=1-348.
DR PDB; 3CCM; X-ray; 2.55 A; G=1-348.
DR PDB; 3CCQ; X-ray; 2.90 A; G=1-348.
DR PDB; 3CCR; X-ray; 3.00 A; G=1-348.
DR PDB; 3CCS; X-ray; 2.95 A; G=1-348.
DR PDB; 3CCU; X-ray; 2.80 A; G=1-348.
DR PDB; 3CCV; X-ray; 2.90 A; G=1-348.
DR PDB; 3CD6; X-ray; 2.75 A; G=1-348.
DR PDB; 3CMA; X-ray; 2.80 A; G=1-348.
DR PDB; 3CME; X-ray; 2.95 A; G=1-348.
DR PDB; 3CPW; X-ray; 2.70 A; G=1-348.
DR PDB; 3CXC; X-ray; 3.00 A; G=1-348.
DR PDB; 3G4S; X-ray; 3.20 A; G=1-348.
DR PDB; 3G6E; X-ray; 2.70 A; G=1-348.
DR PDB; 3G71; X-ray; 2.85 A; G=1-348.
DR PDB; 3I55; X-ray; 3.11 A; G=1-348.
DR PDB; 3I56; X-ray; 2.90 A; G=1-348.
DR PDB; 3OW2; X-ray; 2.70 A; G=12-73.
DR PDB; 4V9F; X-ray; 2.40 A; G=6-211.
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; 4V9F; -.
DR AlphaFoldDB; P15825; -.
DR SMR; P15825; -.
DR IntAct; P15825; 30.
DR STRING; 272569.rrnAC1417; -.
DR DrugCentral; P15825; -.
DR EnsemblBacteria; AAV46344; AAV46344; rrnAC1417.
DR GeneID; 40152384; -.
DR KEGG; hma:rrnAC1417; -.
DR PATRIC; fig|272569.17.peg.2111; -.
DR eggNOG; arCOG04288; Archaea.
DR HOGENOM; CLU_053173_0_0_2; -.
DR OMA; MAHVAEW; -.
DR EvolutionaryTrace; P15825; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR DisProt; DP02536; -.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR HAMAP; MF_00280; Ribosomal_L10_arch; 1.
DR InterPro; IPR022909; 50S_L10_arch.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..348
FT /note="50S ribosomal protein L10"
FT /id="PRO_0000154789"
FT REGION 284..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..342
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 248
FT /note="A -> D (in Ref. 1; CAA35795)"
FT /evidence="ECO:0000305"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2QA4"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:2QA4"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2QA4"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2QA4"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:2QA4"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2QA4"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2QA4"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2QA4"
SQ SEQUENCE 348 AA; 37150 MW; 4063B1C9D2FCB164 CRC64;
MSAESERKTE TIPEWKQEEV DAIVEMIESY ESVGVVNIAG IPSRQLQDMR RDLHGTAELR
VSRNTLLERA LDDVDDGLED LNGYITGQVG LIGTDDNPFS LFQELEASKT PAPIGAGEVA
PNDIVIPEGD TGVDPGPFVG ELQSVGADAR IQEGSIQVLS DSTVLDTGEE VSQELSNVLN
ELGIEPKEVG LDLRAVFADG VLFEPEELEL DIDEYRSDIQ AAAGRAFNLS VNADYPTATT
APTMLQSARG NAKSLALQAA IEDPEVVPDL VSKADAQVRA LASQIDDEEA LPEELQGVEA
DVATEEPTDD QDDDTASEDD ADADDAAEEA DDDDDDDEDA GDALGAMF
