ID A0A0X8FBB5_9LACT Unreviewed; 112 AA.
AC A0A0X8FBB5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Ribonuclease P protein component {ECO:0000256|HAMAP-Rule:MF_00227};
DE Short=RNase P protein {ECO:0000256|HAMAP-Rule:MF_00227};
DE Short=RNaseP protein {ECO:0000256|HAMAP-Rule:MF_00227};
DE EC=3.1.26.5 {ECO:0000256|HAMAP-Rule:MF_00227};
DE AltName: Full=Protein C5 {ECO:0000256|HAMAP-Rule:MF_00227};
GN Name=rnpA {ECO:0000256|HAMAP-Rule:MF_00227};
GN ORFNames=AWM72_04145 {ECO:0000313|EMBL:AMB94009.1}, CYJ28_09150
GN {ECO:0000313|EMBL:PKZ20779.1};
OS Aerococcus sanguinicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=119206 {ECO:0000313|EMBL:AMB94009.1, ECO:0000313|Proteomes:UP000069912};
RN [1] {ECO:0000313|EMBL:AMB94009.1, ECO:0000313|Proteomes:UP000069912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG43001 {ECO:0000313|EMBL:AMB94009.1,
RC ECO:0000313|Proteomes:UP000069912};
RX PubMed=27103727;
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Complete Genome Sequences of Aerococcus christensenii CCUG 28831T,
RT Aerococcus sanguinicola CCUG 43001T, Aerococcus urinae CCUG 36881T,
RT Aerococcus urinaeequi CCUG 28094T, Aerococcus urinaehominis CCUG 42038 BT,
RT and Aerococcus viridans CCUG 4311T.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000069912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG43001 {ECO:0000313|Proteomes:UP000069912};
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Six Aerococcus type strain genome sequencing and assembly using PacBio and
RT Illumina Hiseq.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PKZ20779.1, ECO:0000313|Proteomes:UP000234239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0139 {ECO:0000313|EMBL:PKZ20779.1,
RC ECO:0000313|Proteomes:UP000234239};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from
CC pre-tRNA to produce the mature 5'-terminus. It can also cleave other
CC RNA substrates such as 4.5S RNA. The protein component plays an
CC auxiliary but essential role in vivo by binding to the 5'-leader
CC sequence and broadening the substrate specificity of the ribozyme.
CC {ECO:0000256|ARBA:ARBA00002663, ECO:0000256|HAMAP-Rule:MF_00227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00227};
CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC protein subunit. {ECO:0000256|HAMAP-Rule:MF_00227}.
CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000256|HAMAP-
CC Rule:MF_00227}.
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DR EMBL; CP014160; AMB94009.1; -; Genomic_DNA.
DR EMBL; PKGY01000006; PKZ20779.1; -; Genomic_DNA.
DR RefSeq; WP_067973659.1; NZ_PKGY01000006.1.
DR AlphaFoldDB; A0A0X8FBB5; -.
DR GeneID; 69593932; -.
DR KEGG; asan:AWM72_04145; -.
DR OrthoDB; 9810867at2; -.
DR Proteomes; UP000069912; Chromosome.
DR Proteomes; UP000234239; Unassembled WGS sequence.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00227; RNase_P; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR000100; RNase_P.
DR InterPro; IPR020539; RNase_P_CS.
DR NCBIfam; TIGR00188; rnpA; 1.
DR PANTHER; PTHR33992; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR PANTHER; PTHR33992:SF1; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR Pfam; PF00825; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00227};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00227};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00227};
KW Reference proteome {ECO:0000313|Proteomes:UP000069912};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00227};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00227}.
SQ SEQUENCE 112 AA; 12959 MW; 39308642E3053EAA CRC64;
MRKAYRVKSE ADFGRVFHQG KSTANRQFVV YTIDKEQAHF RLGISVGKKI GNAVTRNYVK
RRIRQSVYEL RDAIRPNQDF IVIARKPTAQ MSMAEIKKSL EHVFNLAGIF KS
//
