ID   RN_BACPU                Reviewed;         162 AA.
AC   P48068;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Ribonuclease;
DE            EC=3.1.27.-;
DE   AltName: Full=RNase Bp;
DE   Flags: Precursor;
OS   Bacillus pumilus (Bacillus mesentericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KMM62;
RX   PubMed=8001670; DOI=10.1016/0014-5793(94)01316-s;
RA   Znamenskaya L.V., Gabdrakhmanova L.A., Chernokalskaya E.B.,
RA   Leshchinskaya I.B., Hartley R.W.;
RT   "Phosphate regulation of biosynthesis of extracellular RNases of endospore-
RT   forming bacteria.";
RL   FEBS Lett. 357:16-18(1995).
CC   -!- FUNCTION: This is a purine-specific ribonuclease.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}.
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DR   EMBL; U06867; AAA75288.1; -; Genomic_DNA.
DR   PIR; S51002; S51002.
DR   RefSeq; WP_044139011.1; NZ_QJIZ01000020.1.
DR   AlphaFoldDB; P48068; -.
DR   SMR; P48068; -.
DR   DrugBank; DB03315; Guanosine 3'-monophosphate.
DR   PATRIC; fig|1408.43.peg.178; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   CDD; cd00933; barnase; 1.
DR   InterPro; IPR001887; Barnase.
DR   InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR   InterPro; IPR016191; Ribonuclease/ribotoxin.
DR   Pfam; PF00545; Ribonuclease; 1.
DR   PIRSF; PIRSF001013; Barnase; 1.
DR   PRINTS; PR00117; BARNASE.
DR   SUPFAM; SSF53933; SSF53933; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..53
FT                   /id="PRO_0000030826"
FT   CHAIN           54..162
FT                   /note="Ribonuclease"
FT                   /id="PRO_0000030827"
FT   ACT_SITE        125
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        154
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   162 AA;  17914 MW;  4555F519F309E297 CRC64;
     MKKISSVFTM FALIAAILFS GFIPQQAYAE TTLTPTATNK TASIQLTSDV HTLAVINTFD
     GVADYLIRYK RLPDNYITKS QASALGWVAS KGNLAEVAPG KSIGGDVFSN REGRLPSASG
     RTWREADINY VSGFRNADRL VYSSDWLIYK TTDHYATFTR IR