PARD1_MYCTU
ID PARD1_MYCTU Reviewed; 83 AA.
AC P9WIJ7; L0T8D6; P67298; P95254;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Antitoxin ParD1;
GN Name=parD1; OrderedLocusNames=Rv1960c; ORFNames=MTCY09F9.04;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP POSSIBLE FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15718296; DOI=10.1093/nar/gki201;
RA Pandey D.P., Gerdes K.;
RT "Toxin-antitoxin loci are highly abundant in free-living but lost from
RT host-associated prokaryotes.";
RL Nucleic Acids Res. 33:966-976(2005).
RN [3]
RP EXPRESSION IN E.COLI, AND FUNCTION AS AN ANTITOXIN.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19016878; DOI=10.1111/j.1574-6968.2008.01400.x;
RA Gupta A.;
RT "Killing activity and rescue function of genome-wide toxin-antitoxin loci
RT of Mycobacterium tuberculosis.";
RL FEMS Microbiol. Lett. 290:45-53(2009).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Upon expression in E.coli neutralizes the effect of cognate toxin
CC ParE1. {ECO:0000269|PubMed:19016878}.
CC -!- SIMILARITY: Belongs to the ParD antitoxin family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44728.1; -; Genomic_DNA.
DR PIR; D70639; D70639.
DR RefSeq; NP_216476.1; NC_000962.3.
DR RefSeq; WP_003409899.1; NZ_NVQJ01000048.1.
DR AlphaFoldDB; P9WIJ7; -.
DR SMR; P9WIJ7; -.
DR STRING; 83332.Rv1960c; -.
DR PaxDb; P9WIJ7; -.
DR DNASU; 885957; -.
DR GeneID; 885957; -.
DR KEGG; mtu:Rv1960c; -.
DR TubercuList; Rv1960c; -.
DR eggNOG; COG3609; Bacteria.
DR OMA; VSAGRYK; -.
DR PhylomeDB; P9WIJ7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0097351; F:toxin sequestering activity; IPI:MTBBASE.
DR GO; GO:0098754; P:detoxification; IMP:MTBBASE.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 6.10.10.120; -; 1.
DR InterPro; IPR022789; ParD.
DR InterPro; IPR038296; ParD_sf.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
DR PANTHER; PTHR36582; PTHR36582; 1.
DR Pfam; PF03693; ParD_antitoxin; 1.
DR SUPFAM; SSF47598; SSF47598; 1.
DR TIGRFAMs; TIGR02606; antidote_CC2985; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..83
FT /note="Antitoxin ParD1"
FT /id="PRO_0000216353"
FT REGION 54..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..60
FT /evidence="ECO:0000255"
SQ SEQUENCE 83 AA; 9239 MW; BC11A37EF0799652 CRC64;
MGKNTSFVLD EHYSAFIDGE IAAGRYRSAS EVIRSALRLL EDRETQLRAL REALEAGERS
GSSTPFDFDG FLGRKRADAS RGR