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RL10_METBF
ID   RL10_METBF              Reviewed;         346 AA.
AC   Q46EU9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 103.
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};
GN   Name=rpl10 {ECO:0000255|HAMAP-Rule:MF_00280};
GN   Synonyms=rplP0 {ECO:0000255|HAMAP-Rule:MF_00280};
GN   OrderedLocusNames=Mbar_A0613;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY.
RX   PubMed=20467040; DOI=10.1074/mcp.m000072-mcp201;
RA   Gordiyenko Y., Videler H., Zhou M., McKay A.R., Fucini P., Biegel E.,
RA   Muller V., Robinson C.V.;
RT   "Mass spectrometry defines the stoichiometry of ribosomal stalk complexes
RT   across the phylogenetic tree.";
RL   Mol. Cell. Proteomics 9:1774-1783(2010).
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:0000255|HAMAP-Rule:MF_00280}.
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 both a pentameric L10(L12)2(L12)2 and heptameric
CC       L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine to
CC       which the L12 dimers bind in a sequential fashion. The proportion of
CC       heptameric complexes increases during cell growth.
CC       {ECO:0000269|PubMed:20467040}.
CC   -!- MASS SPECTROMETRY: Mass=101650.02; Mass_error=30.7;
CC       Method=Electrospray; Note=Isolated L10(L12)6.;
CC       Evidence={ECO:0000269|PubMed:20467040};
CC   -!- MASS SPECTROMETRY: Mass=80124.39; Mass_error=18.0; Method=Electrospray;
CC       Note=Isolated L10(L12)4.; Evidence={ECO:0000269|PubMed:20467040};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00280}.
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DR   EMBL; CP000099; AAZ69593.1; -; Genomic_DNA.
DR   RefSeq; WP_011305644.1; NC_007355.1.
DR   AlphaFoldDB; Q46EU9; -.
DR   SMR; Q46EU9; -.
DR   STRING; 269797.Mbar_A0613; -.
DR   EnsemblBacteria; AAZ69593; AAZ69593; Mbar_A0613.
DR   GeneID; 3627673; -.
DR   KEGG; mba:Mbar_A0613; -.
DR   eggNOG; arCOG04288; Archaea.
DR   HOGENOM; CLU_053173_0_0_2; -.
DR   OMA; MAHVAEW; -.
DR   OrthoDB; 73593at2157; -.
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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..346
FT                   /note="50S ribosomal protein L10"
FT                   /id="PRO_1000006786"
FT   REGION          307..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..335
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   346 AA;  37332 MW;  136B7EE72A436485 CRC64;
     MEEEKHHTEH VPEWKKDEIE NIMELIQSHK VFGMVGIEGI LATKIQKIRR DLKDVAVLKV
     SRNSLTERAL NQLGESIPEM NKYLDKQTAL VFTNESPFKL YKVLEQTKTP SPIKGGAIAP
     ADIIVQKGPT SFPPGPILGE LQSAGIPASI DAGKVAVKET KVVCKAGEVV SQKLATMLTK
     LEIYPLIVGL DLRAVYDNGA IYEPELLAID ESQYFSDITR AAQSAFNLAV NTAYPTSATI
     GTLLAKAFAE SKNLGVNAVV FDSGVMDALL AKAHVQMTSV ASEAADKDAN AVDDQLREVL
     GAAASAAAAV AKEPEKKEEV KEEEEEEEEE DHSEEDGMAG LGSLFG
 
 
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