RL7A_METMP
ID RL7A_METMP Reviewed; 117 AA.
AC P62426;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=50S ribosomal protein L7Ae {ECO:0000255|HAMAP-Rule:MF_00326};
DE AltName: Full=Ribonuclease P protein component Rpp38;
DE Short=RNase P component Rpp38;
DE EC=3.1.26.5;
DE AltName: Full=Ribosomal protein L8e {ECO:0000255|HAMAP-Rule:MF_00326};
GN Name=rpl7ae {ECO:0000255|HAMAP-Rule:MF_00326}; OrderedLocusNames=MMP0641;
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 FUNCTION IN RNASE P, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 32-ASN--LYS-36.
RC STRAIN=S2 / LL;
RX PubMed=20675586; DOI=10.1073/pnas.1005556107;
RA Cho I.M., Lai L.B., Susanti D., Mukhopadhyay B., Gopalan V.;
RT "Ribosomal protein L7Ae is a subunit of archaeal RNase P.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14573-14578(2010).
CC -!- FUNCTION: Multifunctional RNA-binding protein that recognizes the K-
CC turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA,
CC box C/D and box C'/D' sRNAs (By similarity). Part of ribonuclease P, a
CC protein complex that generates mature tRNA molecules by cleaving their
CC 5'-ends, this subunit dramatically stimulates RNase P activity.
CC {ECO:0000255|HAMAP-Rule:MF_00326, ECO:0000269|PubMed:20675586}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for pre-tRNA-Tyr in the absence of L7Ae
CC {ECO:0000269|PubMed:20675586};
CC KM=0.044 uM for pre-tRNA-Tyr in the presence of L7Ae
CC {ECO:0000269|PubMed:20675586};
CC Note=kcat 10 min(-1) in absence of L7Ae, 63 min(-1) in presence of
CC L7Ae. Kinetic parameters determined at 37 degrees Celsius.;
CC Temperature dependence:
CC Optimum temperature is 36-38 degrees Celsius in the absence of L7Ae,
CC 48-50 degrees Celsius in presence of L7Ae.
CC {ECO:0000269|PubMed:20675586};
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Part of the RNase P
CC complex. {ECO:0000269|PubMed:20675586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00326,
CC ECO:0000269|PubMed:20675586}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000255|HAMAP-Rule:MF_00326}.
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DR EMBL; BX950229; CAF30197.1; -; Genomic_DNA.
DR RefSeq; WP_011170585.1; NC_005791.1.
DR AlphaFoldDB; P62426; -.
DR SMR; P62426; -.
DR DIP; DIP-59367N; -.
DR IntAct; P62426; 1.
DR STRING; 267377.MMP0641; -.
DR EnsemblBacteria; CAF30197; CAF30197; MMP0641.
DR GeneID; 37866059; -.
DR GeneID; 5738755; -.
DR KEGG; mmp:MMP0641; -.
DR PATRIC; fig|267377.15.peg.658; -.
DR eggNOG; arCOG01751; Archaea.
DR HOGENOM; CLU_084513_4_0_2; -.
DR OMA; KPFYVRF; -.
DR BRENDA; 3.1.26.5; 3262.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030677; C:ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR Gene3D; 3.30.1330.30; -; 1.
DR HAMAP; MF_00326; Ribosomal_L7Ae_Arch; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR022481; Ribosomal_L7Ae_arc.
DR InterPro; IPR000948; Ribosomal_L7Ae_prok.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00884; RIBOSOMALHS6.
DR SUPFAM; SSF55315; SSF55315; 1.
DR TIGRFAMs; TIGR03677; eL8_ribo; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW tRNA processing.
FT CHAIN 1..117
FT /note="50S ribosomal protein L7Ae"
FT /id="PRO_0000136796"
FT MUTAGEN 32..36
FT /note="NEVTK->AAVTA: 4% of activity in reconstituting RNase
FT P."
FT /evidence="ECO:0000269|PubMed:20675586"
SQ SEQUENCE 117 AA; 12381 MW; DE09BDBC9ACA234A CRC64;
MAVYVKFEIS QELEEKTAEV VANAEKIKKG ANEVTKAVEK GIAKLVVIAQ DVQPEEIVAH
IPVICDEKGI AYSYSSTKEA LGKAAGLEVP TSAIAVVAEG SADELKDLVE KLNGLKA