RL10_METST
ID RL10_METST Reviewed; 332 AA.
AC Q2NEW2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=Msp_1264;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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 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. {ECO:0000255|HAMAP-Rule:MF_00280}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000255|HAMAP-Rule:MF_00280}.
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DR EMBL; CP000102; ABC57641.1; -; Genomic_DNA.
DR RefSeq; WP_011406840.1; NC_007681.1.
DR AlphaFoldDB; Q2NEW2; -.
DR SMR; Q2NEW2; -.
DR STRING; 339860.Msp_1264; -.
DR PRIDE; Q2NEW2; -.
DR EnsemblBacteria; ABC57641; ABC57641; Msp_1264.
DR GeneID; 41325834; -.
DR KEGG; mst:Msp_1264; -.
DR eggNOG; arCOG04288; Archaea.
DR HOGENOM; CLU_053173_0_0_2; -.
DR OMA; MAHVAEW; -.
DR OrthoDB; 73593at2157; -.
DR Proteomes; UP000001931; 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 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..332
FT /note="50S ribosomal protein L10"
FT /id="PRO_1000006792"
FT REGION 294..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..321
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 35543 MW; F0E14E73251020D0 CRC64;
MHHVADWKKE KVAELEDLTN SHEIIGIVNL ADIPAKQLQT MRKSLGDNAI LKMSRKNFIK
IALENSDKEE VEGLADYLEG QPAMVFTKMN PFKLFKILED SKTEAPAKAG SIAPADIVVP
AGDTSFPPGP ILGELQQVGI PAKIDKGSIV VTDDAKIVDE GEEIPKAVAD ILTKLEIHPM
EVGIDLLAVC EGDTIYTADV LAIDEEETIQ TLANAYQSAI NLSVYAGILN SESAPLLIQK
AARDALNLAI NANILTSETT DKILSKAYAQ MLAVAKLLSS EAIDDELNEK LNSQAAAAPV
AVEDNTEEPE EEEEEEEDAA ESAAAGLGAL FG
