ID   NRNA_STRMU              Reviewed;         310 AA.
AC   Q8DTN6;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Probable bifunctional oligoribonuclease and PAP phosphatase NrnA;
DE            EC=3.1.-.-;
DE   AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase;
DE            Short=PAP phosphatase;
DE   AltName: Full=Probable 3'(2'),5'-bisphosphate nucleotidase;
DE            EC=3.1.3.7;
DE   AltName: Full=nanoRNase;
GN   Name=nrnA; OrderedLocusNames=SMU_1297;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [2]
RP   FUNCTION AS A PAP PHOSPHATASE, COFACTOR, COMPLEMENTATION OF E.COLI CYSQ
RP   MUTANT, OPERON STRUCTURE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=19429620; DOI=10.1128/jb.00184-09;
RA   Zhang J., Biswas I.;
RT   "3'-Phosphoadenosine-5'-phosphate phosphatase activity is required for
RT   superoxide stress tolerance in Streptococcus mutans.";
RL   J. Bacteriol. 191:4330-4340(2009).
RN   [3]
RP   COMPLEMENTATION OF E.COLI ORN MUTANT.
RC   STRAIN=ATCC 700610 / UA159;
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: Probable bifunctional enzyme which has pAp-phosphatase and
CC       may have oligoribonuclease activities. Converts 3'(2')-phosphoadenosine
CC       5'-phosphate (PAP) to AMP. Complementation studies suggest it also has
CC       RNA oligoribonuclease activity, although this has not been shown in
CC       vitro using 5- or 20-mers. Involved in superoxide stress response and
CC       sulfur assimilation. {ECO:0000269|PubMed:19429620}.
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:19429620};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:19429620};
CC   -!- DISRUPTION PHENOTYPE: Increased sensitivity to superoxide stress
CC       inducers methyl viologen and menadione. Grows poorly in the absence of
CC       cysteine. {ECO:0000269|PubMed:19429620}.
CC   -!- MISCELLANEOUS: Part of the SMU_1296-SMU_1298 (rpmE2) operon.
CC       {ECO:0000305|PubMed:19429620}.
CC   -!- MISCELLANEOUS: Is able to complement a cysQ mutant in E.coli.
CC       {ECO:0000305|PubMed:19429620}.
CC   -!- SIMILARITY: Belongs to the NrnA oligoribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AE014133; AAN58974.1; -; Genomic_DNA.
DR   RefSeq; NP_721668.1; NC_004350.2.
DR   RefSeq; WP_002263149.1; NC_004350.2.
DR   AlphaFoldDB; Q8DTN6; -.
DR   SMR; Q8DTN6; -.
DR   STRING; 210007.SMU_1297; -.
DR   PRIDE; Q8DTN6; -.
DR   EnsemblBacteria; AAN58974; AAN58974; SMU_1297.
DR   GeneID; 66817310; -.
DR   KEGG; smu:SMU_1297; -.
DR   PATRIC; fig|210007.7.peg.1162; -.
DR   eggNOG; COG0618; Bacteria.
DR   HOGENOM; CLU_039720_1_0_9; -.
DR   OMA; YTGIMTD; -.
DR   PhylomeDB; Q8DTN6; -.
DR   Proteomes; UP000002512; 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; Stress response.
FT   CHAIN           1..310
FT                   /note="Probable bifunctional oligoribonuclease and PAP
FT                   phosphatase NrnA"
FT                   /id="PRO_0000419754"
SQ   SEQUENCE   310 AA;  34625 MW;  17CE936D05E83587 CRC64;
     MTAFKTILAK IKAYDTIIIH RHMKPDPDAL GSQVGLKEMI TSNFPQKTVK VTGYNEPSLS
     WLAQMDDVSD KDYEGALVIV VDTANRPRID DQRYLNGNFL IKIDHHPDED HYGDLSYVDT
     KASSASEIIT DFALQNQLKL SDQAARLLYA GILGDTGRFL YPATTSKTFI IASELLKYDF
     DFAALARQMD SFPYKIAKLQ AYVFENLEID KNGAARIILS QKILKKFNLT DAETSAIVSS
     PGKIDTVQVW AIFVEQADGH YRVRLRSKST VINEVAKRHA GGGHPLASGA NSYSLAENED
     IYQELKNLLK