NRNA_BACSU
ID NRNA_BACSU Reviewed; 313 AA.
AC O34600; Q795V2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=nanoRNase;
GN Name=nrnA; Synonyms=ytqI; OrderedLocusNames=BSU29250;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=168;
RX PubMed=17586819; DOI=10.1093/nar/gkm462;
RA Mechold U., Fang G., Ngo S., Ogryzko V., Danchin A.;
RT "YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase
RT activity.";
RL Nucleic Acids Res. 35:4552-4561(2007).
RN [4]
RP FUNCTION AS AN EXONUCLEASE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=168;
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 [5]
RP FUNCTION AS A DNA OLIGONUCLEASE.
RC STRAIN=168;
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).
RN [6]
RP PRELIMINARY CRYSTALLIZATION.
RX PubMed=22102036; DOI=10.1107/s1744309111026509;
RA Nelersa C.M., Schmier B.J., Malhotra A.;
RT "Purification and crystallization of Bacillus subtilis NrnA, a novel enzyme
RT involved in nanoRNA degradation.";
RL Acta Crystallogr. F 67:1235-1238(2011).
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 3-mers.
CC Directionality is controversial; shown to degrade 5-mers and less in a
CC 3' to 5' direction (PubMed:17586819), 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:17586819,
CC ECO:0000269|PubMed:21087930, 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 Evidence={ECO:0000269|PubMed:17586819};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17586819, ECO:0000269|PubMed:21087930};
CC -!- SUBUNIT: Tetramer. {ECO:0000305|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}.
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DR EMBL; AF008220; AAC00337.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14885.1; -; Genomic_DNA.
DR PIR; F69999; F69999.
DR RefSeq; NP_390803.1; NC_000964.3.
DR RefSeq; WP_004398971.1; NZ_JNCM01000036.1.
DR PDB; 5IPP; X-ray; 1.95 A; A/B/C/D=1-313.
DR PDB; 5IUF; X-ray; 1.95 A; A/B/C/D=1-313.
DR PDB; 5IZO; X-ray; 1.95 A; A/B/C/D=1-313.
DR PDB; 5J21; X-ray; 2.00 A; A/B/C/D=1-313.
DR PDBsum; 5IPP; -.
DR PDBsum; 5IUF; -.
DR PDBsum; 5IZO; -.
DR PDBsum; 5J21; -.
DR AlphaFoldDB; O34600; -.
DR SMR; O34600; -.
DR IntAct; O34600; 1.
DR STRING; 224308.BSU29250; -.
DR jPOST; O34600; -.
DR PaxDb; O34600; -.
DR EnsemblBacteria; CAB14885; CAB14885; BSU_29250.
DR GeneID; 935963; -.
DR KEGG; bsu:BSU29250; -.
DR PATRIC; fig|224308.179.peg.3178; -.
DR eggNOG; COG0618; Bacteria.
DR InParanoid; O34600; -.
DR OMA; YTGIMTD; -.
DR PhylomeDB; O34600; -.
DR BioCyc; BSUB:BSU29250-MON; -.
DR SABIO-RK; O34600; -.
DR Proteomes; UP000001570; 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 3D-structure; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..313
FT /note="Bifunctional oligoribonuclease and PAP phosphatase
FT NrnA"
FT /id="PRO_0000360826"
FT HELIX 1..11
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 25..41
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:5IPP"
FT TURN 55..60
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:5IPP"
FT TURN 157..161
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:5IPP"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:5IPP"
FT HELIX 295..309
FT /evidence="ECO:0007829|PDB:5IPP"
SQ SEQUENCE 313 AA; 35084 MW; 9427328B4D7EA4E5 CRC64;
MKTELIRTIS LYDTIILHRH VRPDPDAYGS QCGLTEILRE TYPEKNIFAV GTPEPSLSFL
YSLDEVDNET YEGALVIVCD TANQERIDDQ RYPSGAKLMK IDHHPNEDPY GDLLWVDTSA
SSVSEMIYEL YLEGKEHGWK LNTKAAELIY AGIVGDTGRF LFPNTTEKTL KYAGELIQYP
FSSSELFNQL YETKLNVVKL NGFIFQNVSL SENGAASVFI KKDTLEKFGT TASEASQLVG
TLGNISGIRA WVFFVEEDDQ IRVRFRSKGP VINGLARKYN GGGHPLASGA SIYSWDEADR
ILADLETLCK EHE
