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   27-MAR-2024, entry version 153.
DE   RecName: Full=Large ribosomal subunit protein uL10 {ECO:0000255|HAMAP-Rule:MF_00280};
DE   AltName: Full=50S ribosomal protein L10 {ECO:0000305};
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   PaxDb; 272569-rrnAC1417; -.
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   EvolutionaryTrace; P15825; -.
DR   Proteomes; UP000001169; Chromosome I.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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   CDD; cd05795; Ribosomal_P0_L10e; 1.
DR   DisProt; DP02536; -.
DR   Gene3D; 3.30.70.1730; -; 1.
DR   Gene3D; 3.90.105.20; -; 1.
DR   Gene3D; 6.10.140.760; -; 1.
DR   HAMAP; MF_00280; Ribosomal_uL10_arch; 1.
DR   InterPro; IPR001790; Ribosomal_uL10.
DR   InterPro; IPR040637; Ribosomal_uL10-like_insert.
DR   InterPro; IPR043164; Ribosomal_uL10-like_insert_sf.
DR   InterPro; IPR043141; Ribosomal_uL10-like_sf.
DR   InterPro; IPR022909; Ribosomal_uL10_arc.
DR   PANTHER; PTHR45699; 60S ACIDIC RIBOSOMAL PROTEIN P0; 1.
DR   PANTHER; PTHR45699:SF3; 60S ACIDIC RIBOSOMAL PROTEIN P0; 1.
DR   Pfam; PF00466; Ribosomal_L10; 1.
DR   Pfam; PF17777; RL10P_insert; 1.
DR   SUPFAM; SSF160369; Ribosomal protein L10-like; 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="Large ribosomal subunit protein uL10"
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
//