NRNA_MYCPN
ID NRNA_MYCPN Reviewed; 324 AA.
AC P75144; Q50340;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Bifunctional oligoribonuclease and PAP phosphatase NrnA;
DE EC=3.1.-.-;
DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase;
DE EC=3.1.3.7;
DE AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase;
DE Short=PAP phosphatase;
DE AltName: Full=Mgp-operon protein 1;
DE Short=Mgp1;
DE AltName: Full=ORF-1 protein;
DE AltName: Full=nanoRNase;
GN Name=nrnA; OrderedLocusNames=MPN_140; ORFNames=MP014;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-324.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=2468577; DOI=10.1016/0378-1119(88)90323-x;
RA Inamine J.M., Loechel S., Hu P.C.;
RT "Analysis of the nucleotide sequence of the P1 operon of Mycoplasma
RT pneumoniae.";
RL Gene 73:175-183(1988).
RN [3]
RP FUNCTION AS AN EXONUCLEASE, FUNCTION AS A PAP PHOSPHATASE,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=21087930; DOI=10.1074/jbc.m110.161596;
RA Wakamatsu T., Kim K., Uemura Y., Nakagawa N., Kuramitsu S., Masui R.;
RT "Role of RecJ-like protein with 5'-3' exonuclease activity in
RT oligo(deoxy)nucleotide degradation.";
RL J. Biol. Chem. 286:2807-2816(2011).
RN [4]
RP FUNCTION AS AN OLIGORIBONUCLEASE, FUNCTION AS A PAP PHOSPHATASE, COFACTOR,
RP AND MUTAGENESIS OF 118-ASP--HIS-120.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=22114320; DOI=10.1261/rna.029132.111;
RA Postic G., Danchin A., Mechold U.;
RT "Characterization of NrnA homologs from Mycobacterium tuberculosis and
RT Mycoplasma pneumoniae.";
RL RNA 18:155-165(2012).
CC -!- FUNCTION: Bifunctional enzyme which has both oligoribonuclease and pAp-
CC phosphatase activities. Degrades RNA and DNA oligonucleotides with a
CC length of 5 nucleotides and shorter, with a preference for longer
CC oligomers. Also degrades 11- and 24-mers, but less efficiently.
CC Directionality is controversial; shown to degrade 5-mers and less in a
CC 3' to 5' direction (PubMed:22114320), and 11-mers in a 5' to 3'
CC direction (PubMed:21087930). Converts 3'(2')-phosphoadenosine 5'-
CC phosphate (PAP) to AMP. {ECO:0000269|PubMed:21087930,
CC ECO:0000269|PubMed:22114320}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:21087930, ECO:0000269|PubMed:22114320};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21087930, ECO:0000269|PubMed:22114320};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21087930, ECO:0000269|PubMed:22114320};
CC Note=Divalent metal cations; Co(2+), Mn(2+) or Mg(2+).
CC {ECO:0000269|PubMed:21087930, ECO:0000269|PubMed:22114320};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.75 uM for ssDNA 6-mers in the presence of Mg(2+)
CC {ECO:0000269|PubMed:21087930};
CC KM=1.5 uM for ssDNA 6-mers in the presence of Mn(2+)
CC {ECO:0000269|PubMed:21087930};
CC KM=0.32 uM for ssRNA 6-mers in the presence of Mg(2+)
CC {ECO:0000269|PubMed:21087930};
CC KM=0.96 uM for ssRNA 6-mers in the presence of Mn(2+)
CC {ECO:0000269|PubMed:21087930};
CC KM=3.5 uM for ssDNA 11-mers in the presence of Mn(2+)
CC {ECO:0000269|PubMed:21087930};
CC KM=2.9 uM for ssRNA 11-mers in the presence of Mn(2+)
CC {ECO:0000269|PubMed:21087930};
CC KM=32 uM for PAP in the presence of Mn(2+)
CC {ECO:0000269|PubMed:21087930};
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:21087930}.
CC -!- MISCELLANEOUS: In accordance with its dual activities, is able to
CC complement both orn and cysQ mutants in E.coli.
CC -!- SIMILARITY: Belongs to the NrnA oligoribonuclease family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA88324.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00089; AAB95662.1; -; Genomic_DNA.
DR EMBL; M21519; AAA88324.1; ALT_INIT; Genomic_DNA.
DR PIR; S73340; S73340.
DR RefSeq; NP_109828.1; NC_000912.1.
DR RefSeq; WP_010874497.1; NC_000912.1.
DR AlphaFoldDB; P75144; -.
DR SMR; P75144; -.
DR STRING; 272634.MPN_140; -.
DR EnsemblBacteria; AAB95662; AAB95662; MPN_140.
DR GeneID; 66609211; -.
DR KEGG; mpn:MPN_140; -.
DR PATRIC; fig|272634.6.peg.154; -.
DR HOGENOM; CLU_039720_1_0_14; -.
DR OMA; CTRWVES; -.
DR BioCyc; MPNE272634:G1GJ3-235-MON; -.
DR SABIO-RK; P75144; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR003156; DHHA1_dom.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02272; DHHA1; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
PE 1: Evidence at protein level;
KW Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..324
FT /note="Bifunctional oligoribonuclease and PAP phosphatase
FT NrnA"
FT /id="PRO_0000096466"
FT MUTAGEN 118..120
FT /note="DHH->AAA: Loss of activity on 5-mers, 15% activity
FT on 24-mers, no longer complements E.coli orn mutant."
FT /evidence="ECO:0000269|PubMed:22114320"
SQ SEQUENCE 324 AA; 37145 MW; F1BFDC4A4983A1F7 CRC64;
MNSQVHRKGS IAEAVSAIQA HDKIVIFHHI RPDGDCLGAQ HGLARLIQTN FPHKQVFCVG
DPKHNFPWLE MVFTPKEQIT PELMQQALAV IVDANYKERI ECRDLLDQNQ FKAVLRIDHH
PNEDDLNTTH NFVDASYIAA AEQVVDLAVQ AKWKLSPPAA TALYLGIYTD SNRFLYSNTS
WRTLYLGSML YRAQANIAKI HDELNHTSLK DIQFKQYVFK NFQTFQNVIY FVADKKFQKK
LKVTPLECAR VNILANIEQF HIWLFFIEEG KNHYRVEFRS NGINVREVAL KYGGGGHIQA
SGAVLKSKRD IIRVVQDCQK QIAV
