RL10_PYRHO
ID RL10_PYRHO Reviewed; 342 AA.
AC O74109;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=Anchor protein P0;
GN Name=rpl10 {ECO:0000255|HAMAP-Rule:MF_00280};
GN Synonyms=rplP0 {ECO:0000255|HAMAP-Rule:MF_00280}; OrderedLocusNames=PH1999;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, RNA-BINDING, AND SUBUNIT.
RX PubMed=17804412; DOI=10.1074/jbc.m705412200;
RA Maki Y., Hashimoto T., Zhou M., Naganuma T., Ohta J., Nomura T.,
RA Robinson C.V., Uchiumi T.;
RT "Three binding sites for stalk protein dimers are generally present in
RT ribosomes from archaeal organism.";
RL J. Biol. Chem. 282:32827-32833(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 1-284, SUBUNIT, AND MUTAGENESIS
RP OF 217-LEU--ALA-224; 243-ILE--ALA-250 AND 272-ALA--LEU-279.
RX PubMed=20007716; DOI=10.1074/jbc.m109.068098;
RA Naganuma T., Nomura N., Yao M., Mochizuki M., Uchiumi T., Tanaka I.;
RT "Structural basis for translation factor recruitment to the
RT eukaryotic/archaeal ribosomes.";
RL J. Biol. Chem. 285:4747-4756(2010).
CC -!- FUNCTION: Forms the large subunit's ribosomal stalk, playing a central
CC role in the interaction of the ribosome with elongation factors; the
CC stalk complex of P.horikoshii binds to E.coli large subunits and
CC confers on them the ability to interact with eukaryotic elongation
CC factors. Each succesive L12 dimer bound along the P0 spine increases
CC the GTPase activity of elongation factors and increases translation by
CC reconsituted ribosomes, although the first site is the most
CC stimulatory. {ECO:0000269|PubMed:17804412}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit, binds large rRNA. Forms the
CC ribosomal stalk which helps the ribosome interact with GTP-bound
CC translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex,
CC where L10 forms an elongated spine to which the L12 dimers bind in a
CC sequential fashion. {ECO:0000269|PubMed:17804412,
CC ECO:0000269|PubMed:20007716}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000255|HAMAP-Rule:MF_00280}.
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DR EMBL; BA000001; BAA31126.1; -; Genomic_DNA.
DR PIR; G71216; G71216.
DR RefSeq; WP_010886060.1; NC_000961.1.
DR PDB; 3A1Y; X-ray; 2.13 A; G=1-284.
DR PDBsum; 3A1Y; -.
DR AlphaFoldDB; O74109; -.
DR SMR; O74109; -.
DR STRING; 70601.3258443; -.
DR EnsemblBacteria; BAA31126; BAA31126; BAA31126.
DR GeneID; 1442842; -.
DR KEGG; pho:PH1999; -.
DR eggNOG; arCOG04288; Archaea.
DR OMA; MAHVAEW; -.
DR OrthoDB; 73593at2157; -.
DR EvolutionaryTrace; O74109; -.
DR Proteomes; UP000000752; Chromosome.
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 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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..342
FT /note="50S ribosomal protein L10"
FT /id="PRO_0000154804"
FT REGION 212..342
FT /note="Required for interaction with ribosomal protein L12
FT dimers"
FT REGION 299..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 217..224
FT /note="LQKAYMHA->QQKAYMHQ: Binds less L12, about 50% GTPase
FT activity, about 35% GTPase activity; when associated with
FT 243-Q--Q250 or 272-Q--Q-279."
FT /evidence="ECO:0000269|PubMed:20007716"
FT MUTAGEN 243..250
FT /note="IQKAFLNA->QQKAFLNQ: About 65% GTPase activity; when
FT associated with 272-Q--Q-279. About 35% GTPase activity;
FT when associated with 217-Q--Q-224."
FT /evidence="ECO:0000269|PubMed:20007716"
FT MUTAGEN 272..279
FT /note="AFRAMLLL->QFRAMLLQ: About 65% GTPase activity; when
FT associated with 243-Q--Q-250. About 35% GTPase activity;
FT when associated with 217-Q--Q-224."
FT /evidence="ECO:0000269|PubMed:20007716"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:3A1Y"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:3A1Y"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:3A1Y"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:3A1Y"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3A1Y"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:3A1Y"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:3A1Y"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 210..231
FT /evidence="ECO:0007829|PDB:3A1Y"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 239..256
FT /evidence="ECO:0007829|PDB:3A1Y"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 265..280
FT /evidence="ECO:0007829|PDB:3A1Y"
SQ SEQUENCE 342 AA; 37514 MW; A469330FC19E6195 CRC64;
MAHVAEWKKK EVEELAKLIK SYPVIALVDV SSMPAYPLSQ MRRLIRENGG LLRVSRNTLI
ELAIKKAAKE LGKPELEKLV EYIDRGAGIL VTNMNPFKLY KFLQQNRQPA PAKPGAVVPK
DVVVPAGPTP LAPGPIVGQM QALGIPARIE KGKVTIQKDT TVLKAGEVIT PELANILNAL
GIQPLEVGLD VLAVYEDGIV YTPDVLAIDE QEYIDMLQKA YMHAFNLAVN IAYPTPETIE
AIIQKAFLNA KTVAIEAGYI TKETIQDIIG RAFRAMLLLA QQLPEDVLDE KTKELLSAQA
QVAVATQPSE EEKKEEEKTE EEEKEEEASE EEALAGLSAL FG
