RL10_METMP
ID RL10_METMP Reviewed; 335 AA.
AC Q6M0L1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=MMP0259;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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. Homodimer, it forms part of
CC the ribosomal stalk which helps the ribosome interact with GTP-bound
CC translation factors. Forms both a pentameric L10(L12)2(L12)2 and
CC heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated
CC spine to which the L12 dimers bind in a sequential fashion. The
CC proportion of heptameric complexes increases during cell growth.
CC {ECO:0000269|PubMed:20467040}.
CC -!- MASS SPECTROMETRY: Mass=95159.52; Mass_error=15.63;
CC Method=Electrospray; Note=Isolated L10(L12)6.;
CC Evidence={ECO:0000269|PubMed:20467040};
CC -!- MASS SPECTROMETRY: Mass=74814.80; Mass_error=4.99; 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; BX950229; CAF29815.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6M0L1; -.
DR SMR; Q6M0L1; -.
DR STRING; 267377.MMP0259; -.
DR EnsemblBacteria; CAF29815; CAF29815; MMP0259.
DR KEGG; mmp:MMP0259; -.
DR PATRIC; fig|267377.15.peg.261; -.
DR eggNOG; arCOG04288; Archaea.
DR HOGENOM; CLU_053173_0_0_2; -.
DR OMA; MAHVAEW; -.
DR BioCyc; MMAR267377:MMP_RS01400-MON; -.
DR Proteomes; UP000000590; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..335
FT /note="50S ribosomal protein L10"
FT /id="PRO_1000006790"
FT REGION 304..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 35805 MW; 18B57FCBD87A86B8 CRC64;
MIEAKSEHKI APWKIEEVNA LKELLKSSNI IALIDMMEVP AVQLQEIRDK IRDQMTLKMS
RNTLMKRAIE EVAEETGNPE FAKLVDYMDK GAAIIATEMN PFKLYKTLDE SKSPAPVKGG
AIAPCDIEVK AGSTGMPPGP FLSELKAVGI PAAIDKGKIG IKEDKIVVKE GEVVSQKLAV
VLSALDIKPV TVGLNVLGVY EDGVIYTESD LKIDEEEFVG KIQKAYTSAF NLSVNAVIPT
SATVETIVQK AFNDAKAVSV ESAFVTDKTA DAILGKAYAQ MIAVAGLAGD DALDEDLKGK
ISSGAAAPVE EAPVEEKKEE KKEEAAAPAG LGMLF