ID   RNP2_METMP              Reviewed;         130 AA.
AC   P60780;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   04-NOV-2026, entry version 90.
DE   RecName: Full=Ribonuclease P protein component 2 {ECO:0000255|HAMAP-Rule:MF_00755};
DE            Short=RNase P component 2 {ECO:0000255|HAMAP-Rule:MF_00755};
DE            EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00755};
DE   AltName: Full=Pop5 {ECO:0000255|HAMAP-Rule:MF_00755};
GN   Name=rnp2 {ECO:0000255|HAMAP-Rule:MF_00755};
GN   OrderedLocusNames=MMP0878;
OS   Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2
OS   / LL).
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanococci; Methanococcales; Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14266 / JCM 13030 / NBRC 101832 / 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, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=DSM 14266 / JCM 13030 / NBRC 101832 / 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: Part of ribonuclease P, a protein complex that generates
CC       mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-
CC       Rule:MF_00755, 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00755};
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: Consists of a catalytic RNA component and at least 5 protein
CC       subunits. {ECO:0000269|PubMed:20675586}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00755,
CC       ECO:0000269|PubMed:20675586}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 2 family. {ECO:0000255|HAMAP-Rule:MF_00755}.
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DR   EMBL; BX950229; CAF30434.1; -; Genomic_DNA.
DR   RefSeq; WP_011170822.1; NC_005791.1.
DR   SMR; P60780; -.
DR   DIP; DIP-59368N; -.
DR   IntAct; P60780; 1.
DR   STRING; 267377.MMP0878; -.
DR   EnsemblBacteria; CAF30434; CAF30434; MMP0878.
DR   GeneID; 2762695; -.
DR   KEGG; mmp:MMP0878; -.
DR   PATRIC; fig|267377.15.peg.904; -.
DR   eggNOG; arCOG01365; Archaea.
DR   HOGENOM; CLU_137733_1_0_2; -.
DR   OMA; AFELIFQ; -.
DR   OrthoDB; 19261at2157; -.
DR   BRENDA; 3.1.26.5; 3262.
DR   Gene3D; 3.30.70.3250; Ribonuclease P, Pop5 subunit; 1.
DR   HAMAP; MF_00755; RNase_P_2; 1.
DR   InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR   InterPro; IPR038085; Rnp2-like_sf.
DR   PANTHER; PTHR15441; RIBONUCLEASE P PROTEIN SUBUNIT P14; 1.
DR   PANTHER; PTHR15441:SF2; RIBONUCLEASE P_MRP PROTEIN SUBUNIT POP5; 1.
DR   Pfam; PF01900; RNase_P_Rpp14; 1.
DR   PIRSF; PIRSF004952; RNase_P_2; 1.
DR   SUPFAM; SSF160350; Rnp2-like; 1.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030677; C:ribonuclease P complex; IDA:UniProtKB.
DR   GO; GO:0004526; F:ribonuclease P activity; IDA:UniProtKB.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR   Proteomes; UP000000590; Chromosome.
DR   AlphaFoldDB; P60780; -.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..130
FT                   /note="Ribonuclease P protein component 2"
FT                   /id="PRO_0000140023"
SQ   SEQUENCE   130 AA;  15149 MW;  F886926B406FCA75 CRC64;
     MLKTLPPTLR EKKRYVALEI IYEMELSQKD VISVVRNALL NYSGVLGCSR TNPWLIDYGH
     PYGILRISRE EVDTLRSSLS LMGEHKKKPI NIRIIGISNS VKHIREKFLH VPHEPYYKVI
     QKLKRKGPKK
//