ABIQ_LACLL
ID ABIQ_LACLL Reviewed; 183 AA.
AC Q9ZJ19;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Endoribonuclease AbiQ {ECO:0000303|PubMed:23279123};
DE Short=ABIQ {ECO:0000303|PubMed:23279123};
DE EC=3.1.-.-;
DE AltName: Full=Toxin AbiQ {ECO:0000305};
GN Name=abiQ {ECO:0000303|PubMed:9835558};
OS Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG Plasmid pSRQ900.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1360;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=W-37; PLASMID=pSRQ900;
RX PubMed=9835558; DOI=10.1128/aem.64.12.4748-4756.1998;
RA Emond E., Dion E., Walker S.A., Vedamuthu E.R., Kondo J.K., Moineau S.;
RT "AbiQ, an abortive infection mechanism from Lactococcus lactis.";
RL Appl. Environ. Microbiol. 64:4748-4756(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W-37; PLASMID=pSRQ900;
RX PubMed=11467810; DOI=10.3168/jds.s0022-0302(01)74595-x;
RA Boucher I., Emond E., Parrot M., Moineau S.;
RT "DNA sequence analysis of three Lactococcus lactis plasmids encoding phage
RT resistance mechanisms.";
RL J. Dairy Sci. 84:1610-1620(2001).
RN [3]
RP FUNCTION.
RX PubMed=23813728; DOI=10.1128/jb.00296-13;
RA Samson J.E., Belanger M., Moineau S.;
RT "Effect of the abortive infection mechanism and type III toxin/antitoxin
RT system AbiQ on the lytic cycle of Lactococcus lactis phages.";
RL J. Bacteriol. 195:3947-3956(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 13-183, FUNCTION, INDUCTION, AND
RP MUTAGENESIS OF TYR-38; PRO-60; SER-62; SER-63; LYS-65; LYS-66; LYS-71;
RP ARG-78 AND ARG-80.
RX PubMed=23279123; DOI=10.1111/mmi.12129;
RA Samson J.E., Spinelli S., Cambillau C., Moineau S.;
RT "Structure and activity of AbiQ, a lactococcal endoribonuclease belonging
RT to the type III toxin-antitoxin system.";
RL Mol. Microbiol. 87:756-768(2013).
CC -!- FUNCTION: Toxic component of a type III toxin-antitoxin (TA) system. An
CC endoribonuclease that is probably sequence-specific. It is neutralized
CC by its cognate antitoxin RNA AntiQ, which has 2.8 35 nucleotide-long
CC repeats. Cannot be cloned in L.lactis subsp. cremoris strain NZ9000 in
CC the absence of the antitoxin gene; expression in strain NZ9000 even in
CC the presence of antiQ inhibits growth in a bacteriostatic fashion
CC (PubMed:23279123). Confers resistance to 936 and c2 phages but not P335
CC phages in L.lactis, causes an abortive infection (Abi phenotype). Viral
CC DNA is replicated but not cleaved from its concatemeric form, while the
CC viral major structural protein is produced normally in the presence of
CC this protein (PubMed:9835558). Operon expression in E.coli confers
CC resistance to 3 phages of the Myoviridae family (T4, RB69 and phage 2)
CC and 1 of the Siphoviridae family (T5), but not other tested phages (T1,
CC T3, lambda vir, HK97, Mu and pilH alpha). The presence of this operon
CC in L.lactis subsp. lactis strain IL1403 during phage P008 infection
CC alters the viral transcription profiles (PubMed:23813728).
CC {ECO:0000269|PubMed:23279123, ECO:0000269|PubMed:23813728,
CC ECO:0000269|PubMed:9835558}.
CC -!- SUBUNIT: Forms a triangular heterohexamer with a single 35-nt-long
CC repeat of RNA antitoxin AntiQ. {ECO:0000250|UniProtKB:B8X8Z0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9835558}.
CC -!- INDUCTION: Constitutively expressed in the presence or absence of phage
CC P0008 (in L.lactis subsp. lactis strain IL1403) (at protein level); in
CC the presence of phage the abiQ transcript level decreases while the
CC antiQ transcript does not. Part of the antiQ-abiQ operon.
CC {ECO:0000269|PubMed:23279123}.
CC -!- DISRUPTION PHENOTYPE: Loss of resistance to bacteriophage.
CC {ECO:0000269|PubMed:9835558}.
CC -!- SIMILARITY: Belongs to the ToxN/AbiQ toxin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
CC {ECO:0000305|PubMed:23279123}.
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DR EMBL; AF001314; AAC98713.1; -; Genomic_DNA.
DR RefSeq; NP_862552.1; NC_004959.1.
DR PDB; 4GLK; X-ray; 2.16 A; A=13-183.
DR PDBsum; 4GLK; -.
DR AlphaFoldDB; Q9ZJ19; -.
DR SMR; Q9ZJ19; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:CACAO.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR025911; ToxN/AbiQ_toxin.
DR Pfam; PF13958; ToxN_toxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Endonuclease; Hydrolase;
KW Nuclease; Plasmid; Toxin-antitoxin system.
FT CHAIN 1..183
FT /note="Endoribonuclease AbiQ"
FT /id="PRO_0000432894"
FT MUTAGEN 38
FT /note="Y->A,C: Loss of resistance of phage P0008, still has
FT RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT MUTAGEN 60
FT /note="P->L: Loss of resistance of phage P0008, slightly
FT decreased RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT MUTAGEN 62
FT /note="S->L: Loss of resistance of phage P0008, loss of
FT RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT MUTAGEN 62
FT /note="S->T: Loss of resistance of phage P0008, still has
FT RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT MUTAGEN 63
FT /note="S->A: Loss of resistance of phage P0008, slightly
FT decreased RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT MUTAGEN 65
FT /note="K->A: Loss of resistance of phage P0008, still has
FT RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT MUTAGEN 66
FT /note="K->A: Wild-type; retains resistance to phage P0008,
FT still has RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT MUTAGEN 71
FT /note="K->A: Loss of resistance of phage P0008, still has
FT RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT MUTAGEN 78
FT /note="R->E: Loss of resistance of phage P0008, decreased
FT RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT MUTAGEN 80
FT /note="R->E: Wild-type; retains resistance to phage P0008,
FT still has RNase activity."
FT /evidence="ECO:0000269|PubMed:23279123"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4GLK"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:4GLK"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:4GLK"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:4GLK"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:4GLK"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:4GLK"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:4GLK"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4GLK"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:4GLK"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4GLK"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4GLK"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4GLK"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:4GLK"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:4GLK"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:4GLK"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:4GLK"
SQ SEQUENCE 183 AA; 21723 MW; FC032C690AF15B35 CRC64;
MSSFFYKEIL RMTLRFFTVT DEYIAYLRKF ESKVHYQYEN NASTYVGVVL KKNDFNYFIP
LSSYKKGNPE KDKAMKKRSR IVTRLFEIGN INNPLGYLLH HNMIPVPDSE LIPLPLDLKK
PKHKMMQKQL IYMKSISEKI ENKSEVVYRK AAHEKDGYYL KFSCDFKLLE AKATLYSKKS
TFQ
