ID   RNBR_BACAM              Reviewed;         157 AA.
AC   P00648;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=Ribonuclease;
DE            EC=3.1.27.-;
DE   AltName: Full=Barnase;
DE   AltName: Full=RNase Ba;
DE   Flags: Precursor;
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3007290; DOI=10.1016/0378-1119(85)90045-9;
RA   Paddon C.J., Hartley R.W.;
RT   "Cloning, sequencing and transcription of an inactivated copy of Bacillus
RT   amyloliquefaciens extracellular ribonuclease (barnase).";
RL   Gene 40:231-239(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-157.
RX   PubMed=3050134; DOI=10.1016/0022-2836(88)90568-2;
RA   Hartley R.W.;
RT   "Barnase and barstar. Expression of its cloned inhibitor permits expression
RT   of a cloned ribonuclease.";
RL   J. Mol. Biol. 202:913-915(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 48-157.
RX   PubMed=4553460; DOI=10.1038/newbio235015a0;
RA   Hartley R.W., Barker E.A.;
RT   "Amino-acid sequence of extracellular ribonuclease (barnase) of Bacillus
RT   amyloliquefaciens.";
RL   Nature New Biol. 235:15-16(1972).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=1888730; DOI=10.1021/bi00099a030;
RA   Bycroft M., Ludvigsen S., Fersht A.R., Poulsen F.M.;
RT   "Determination of the three-dimensional solution structure of barnase using
RT   nuclear magnetic resonance spectroscopy.";
RL   Biochemistry 30:8697-8701(1991).
RN   [5]
RP   STRUCTURE BY NMR OF 48-83.
RX   PubMed=1569554; DOI=10.1016/0022-2836(92)90559-3;
RA   Sancho J., Neira J.L., Fersht A.R.;
RT   "An N-terminal fragment of barnase has residual helical structure similar
RT   to that in a refolding intermediate.";
RL   J. Mol. Biol. 224:749-758(1992).
RN   [6]
RP   STRUCTURE BY NMR OF 48-157.
RX   PubMed=9708913; DOI=10.1016/s0014-5793(98)00765-0;
RA   Reibarkh M.Y.A., Nolde D.E., Vasilieva L.I., Bocharov E.V., Shulga A.A.,
RA   Kirpichnikov M.P., Arseniev A.S.;
RT   "Three-dimensional structure of binase in solution.";
RL   FEBS Lett. 431:250-254(1998).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=2023257; DOI=10.1016/0022-2836(91)90862-z;
RA   Baudet S., Janin J.;
RT   "Crystal structure of a barnase-d(GpC) complex at 1.9-A resolution.";
RL   J. Mol. Biol. 219:123-132(1991).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH BARNASE.
RX   PubMed=16100951; DOI=10.1016/0969-2126(93)90018-c;
RA   Guillet V., Lapthorn A., Hartley R.W., Mauguen Y.;
RT   "Recognition between a bacterial ribonuclease, barnase, and its natural
RT   inhibitor, barstar.";
RL   Structure 1:165-177(1993).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=11914482; DOI=10.1107/s0907444902001567;
RA   Vaughan C.K., Harryson P., Buckle A.M., Fersht A.R.;
RT   "A structural double-mutant cycle: estimating the strength of a buried salt
RT   bridge in barnase.";
RL   Acta Crystallogr. D 58:591-600(2002).
RN   [10]
RP   REVIEW.
RX   PubMed=2696173; DOI=10.1016/0968-0004(89)90104-7;
RA   Hartley R.W.;
RT   "Barnase and barstar: two small proteins to fold and fit together.";
RL   Trends Biochem. Sci. 14:450-454(1989).
CC   -!- FUNCTION: Hydrolyzes phosphodiester bonds in RNA, poly- and
CC       oligoribonucleotides resulting in 3'-nucleoside monophosphates via
CC       2',3'-cyclophosphate intermediates.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in male
CC       sterile maize and rape by Plant Genetic Systems and in radicchio rosso
CC       by Bejo Zaden. Barnase expressed in transgenic plants will specifically
CC       destroy the tissue(s) where it is expressed. After cell transformation,
CC       protein expression and plant regeneration, the active nuclease destroys
CC       the pollen producing organs thus rendering the plant sterile.
CC   -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}.
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DR   EMBL; M14442; AAA86441.1; -; Genomic_DNA.
DR   EMBL; X12871; CAA31365.1; -; Genomic_DNA.
DR   PIR; A24038; NRBSN.
DR   PDB; 1A2P; X-ray; 1.50 A; A/B/C=48-157.
DR   PDB; 1B20; X-ray; 1.70 A; A/B/C=48-157.
DR   PDB; 1B21; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1B27; X-ray; 2.10 A; A/B/C=48-157.
DR   PDB; 1B2S; X-ray; 1.82 A; A/B/C=48-157.
DR   PDB; 1B2U; X-ray; 2.10 A; A/B/C=48-157.
DR   PDB; 1B2X; X-ray; 1.80 A; A/B/C=48-157.
DR   PDB; 1B2Z; X-ray; 2.03 A; A/B/C=48-157.
DR   PDB; 1B3S; X-ray; 2.39 A; A/B/C=48-157.
DR   PDB; 1BAN; X-ray; 2.20 A; A/B/C=48-157.
DR   PDB; 1BAO; X-ray; 2.20 A; A/B/C=48-157.
DR   PDB; 1BGS; X-ray; 2.60 A; A/B/C=48-157.
DR   PDB; 1BNE; X-ray; 2.10 A; A/B/C=48-157.
DR   PDB; 1BNF; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1BNG; X-ray; 2.10 A; A/B/C=48-157.
DR   PDB; 1BNI; X-ray; 2.10 A; A/B/C=48-157.
DR   PDB; 1BNJ; X-ray; 2.10 A; A/B/C=48-157.
DR   PDB; 1BNR; NMR; -; A=48-157.
DR   PDB; 1BNS; X-ray; 2.05 A; A/B/C=48-157.
DR   PDB; 1BRG; X-ray; 2.20 A; A/B/C=50-157.
DR   PDB; 1BRH; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1BRI; X-ray; 1.90 A; A/B/C=48-157.
DR   PDB; 1BRJ; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1BRK; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1BRN; X-ray; 1.76 A; L/M=48-157.
DR   PDB; 1BRS; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1BSA; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1BSB; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1BSC; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1BSD; X-ray; 2.30 A; A/B/C=48-157.
DR   PDB; 1BSE; X-ray; 2.00 A; A/B/C=48-157.
DR   PDB; 1FW7; NMR; -; A=48-157.
DR   PDB; 1RNB; X-ray; 1.90 A; A=48-157.
DR   PDB; 1X1U; X-ray; 2.30 A; A/B/C=48-157.
DR   PDB; 1X1W; X-ray; 2.10 A; A/B/C=48-157.
DR   PDB; 1X1X; X-ray; 2.30 A; A/B/C=48-157.
DR   PDB; 1X1Y; X-ray; 1.90 A; A/B/C=48-157.
DR   PDB; 1YVS; X-ray; 2.20 A; A=48-157.
DR   PDB; 2C4B; X-ray; 1.30 A; A/B=49-157.
DR   PDB; 2F4Y; X-ray; 2.15 A; A/B/C=50-157.
DR   PDB; 2F56; X-ray; 1.96 A; A/B/C=50-157.
DR   PDB; 2F5M; X-ray; 1.95 A; A/B/C=50-157.
DR   PDB; 2F5W; X-ray; 2.00 A; A/B/C=50-157.
DR   PDB; 2KF3; NMR; -; A=48-157.
DR   PDB; 2KF4; NMR; -; A=48-157.
DR   PDB; 2KF5; NMR; -; A=48-157.
DR   PDB; 2KF6; NMR; -; A=48-157.
DR   PDB; 2ZA4; X-ray; 1.58 A; A/C=48-157.
DR   PDB; 3DA7; X-ray; 2.25 A; A/B/E/G=48-113.
DR   PDB; 3KCH; X-ray; 1.94 A; A/B/C=48-157.
DR   PDB; 3Q3F; X-ray; 2.17 A; A=48-157.
DR   PDB; 6PQK; X-ray; 1.20 A; A/C=48-157.
DR   PDB; 7MRX; X-ray; 2.29 A; A/C/E=48-157.
DR   PDBsum; 1A2P; -.
DR   PDBsum; 1B20; -.
DR   PDBsum; 1B21; -.
DR   PDBsum; 1B27; -.
DR   PDBsum; 1B2S; -.
DR   PDBsum; 1B2U; -.
DR   PDBsum; 1B2X; -.
DR   PDBsum; 1B2Z; -.
DR   PDBsum; 1B3S; -.
DR   PDBsum; 1BAN; -.
DR   PDBsum; 1BAO; -.
DR   PDBsum; 1BGS; -.
DR   PDBsum; 1BNE; -.
DR   PDBsum; 1BNF; -.
DR   PDBsum; 1BNG; -.
DR   PDBsum; 1BNI; -.
DR   PDBsum; 1BNJ; -.
DR   PDBsum; 1BNR; -.
DR   PDBsum; 1BNS; -.
DR   PDBsum; 1BRG; -.
DR   PDBsum; 1BRH; -.
DR   PDBsum; 1BRI; -.
DR   PDBsum; 1BRJ; -.
DR   PDBsum; 1BRK; -.
DR   PDBsum; 1BRN; -.
DR   PDBsum; 1BRS; -.
DR   PDBsum; 1BSA; -.
DR   PDBsum; 1BSB; -.
DR   PDBsum; 1BSC; -.
DR   PDBsum; 1BSD; -.
DR   PDBsum; 1BSE; -.
DR   PDBsum; 1FW7; -.
DR   PDBsum; 1RNB; -.
DR   PDBsum; 1X1U; -.
DR   PDBsum; 1X1W; -.
DR   PDBsum; 1X1X; -.
DR   PDBsum; 1X1Y; -.
DR   PDBsum; 1YVS; -.
DR   PDBsum; 2C4B; -.
DR   PDBsum; 2F4Y; -.
DR   PDBsum; 2F56; -.
DR   PDBsum; 2F5M; -.
DR   PDBsum; 2F5W; -.
DR   PDBsum; 2KF3; -.
DR   PDBsum; 2KF4; -.
DR   PDBsum; 2KF5; -.
DR   PDBsum; 2KF6; -.
DR   PDBsum; 2ZA4; -.
DR   PDBsum; 3DA7; -.
DR   PDBsum; 3KCH; -.
DR   PDBsum; 3Q3F; -.
DR   PDBsum; 6PQK; -.
DR   PDBsum; 7MRX; -.
DR   AlphaFoldDB; P00648; -.
DR   BMRB; P00648; -.
DR   SMR; P00648; -.
DR   DIP; DIP-544N; -.
DR   IntAct; P00648; 1.
DR   STRING; 692420.BAMF_3319; -.
DR   eggNOG; COG4290; Bacteria.
DR   BRENDA; 4.6.1.24; 630.
DR   EvolutionaryTrace; P00648; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR   CDD; cd00933; barnase; 1.
DR   Gene3D; 3.40.20.20; -; 2.
DR   InterPro; IPR001887; Barnase.
DR   InterPro; IPR000026; Gua-sp_ribonuclease_Sa-like.
DR   InterPro; IPR016191; Ribonuclease/ribotoxin.
DR   Pfam; PF00545; Ribonuclease; 1.
DR   PIRSF; PIRSF001013; Barnase; 1.
DR   PRINTS; PR00117; BARNASE.
DR   SUPFAM; SSF53933; Microbial ribonucleases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Endonuclease;
KW   Genetically modified food; Hydrolase; Nuclease; Secreted; Signal.
FT   SIGNAL          1..34
FT   PROPEP          35..47
FT                   /evidence="ECO:0000269|PubMed:4553460"
FT                   /id="PRO_0000030828"
FT   CHAIN           48..157
FT                   /note="Ribonuclease"
FT                   /evidence="ECO:0000269|PubMed:4553460"
FT                   /id="PRO_0000030829"
FT   ACT_SITE        120
FT                   /note="Proton acceptor"
FT   ACT_SITE        149
FT                   /note="Proton donor"
FT   MUTAGEN         149
FT                   /note="H->Q: Loss of activity."
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:3DA7"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:3DA7"
FT   HELIX           54..64
FT                   /evidence="ECO:0007829|PDB:6PQK"
FT   HELIX           74..79
FT                   /evidence="ECO:0007829|PDB:6PQK"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:6PQK"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:6PQK"
FT   STRAND          97..103
FT                   /evidence="ECO:0007829|PDB:6PQK"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:6PQK"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:6PQK"
FT   STRAND          134..138
FT                   /evidence="ECO:0007829|PDB:6PQK"
FT   STRAND          143..148
FT                   /evidence="ECO:0007829|PDB:6PQK"
FT   STRAND          154..157
FT                   /evidence="ECO:0007829|PDB:6PQK"
SQ   SEQUENCE   157 AA;  17473 MW;  42B6669F9B0D7FBA CRC64;
     MMKMEGIALK KRLSWISVCL LVLVSAAGML FSTAAKTETS SHKAHTEAQV INTFDGVADY
     LQTYHKLPDN YITKSEAQAL GWVASKGNLA DVAPGKSIGG DIFSNREGKL PGKSGRTWRE
     ADINYTSGFR NSDRILYSSD WLIYKTTDHY QTFTKIR
//