RNBR_BACAM
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 25-MAY-2022, entry version 136.
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; Firmicutes; 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 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 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: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 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
