ID   DOC_MYCS2               Reviewed;         130 AA.
AC   A0QRY0;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Toxin Doc;
DE   AltName: Full=Death on curing protein;
GN   Name=doc; OrderedLocusNames=MSMEG_1278, MSMEI_1240;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION AS A TOXIN, FUNCTION IN TRANSCRIPTION REGULATION, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=22199354; DOI=10.1074/jbc.m111.286856;
RA   Frampton R., Aggio R.B., Villas-Boas S.G., Arcus V.L., Cook G.M.;
RT   "Toxin-antitoxin systems of Mycobacterium smegmatis are essential for cell
RT   survival.";
RL   J. Biol. Chem. 287:5340-5356(2012).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC       Upon overexpression causes bacteriostasis. Its effect is neutralized by
CC       coexpression with cognate antitoxin PhD. May bind the 30S ribosomal
CC       subunit. In M.smegmatis 3 TA systems (VapB-VapC, MazE-MazF and Phd-Doc)
CC       may be involved in monitoring the nutritional supply and physiological
CC       state of the cell, linking catabolic with anabolic reactions.
CC       {ECO:0000269|PubMed:22199354}.
CC   -!- INDUCTION: Constitutively expressed in all growth phases, part of the
CC       MSMEG_1276-phd-doc-MSMEG_1279 operon. Negatively autoregulated by one
CC       or both of Phd-Doc. {ECO:0000269|PubMed:22199354}.
CC   -!- DISRUPTION PHENOTYPE: The phd-doc operon is not essential. A triple TA
CC       mutant (missing vapB-vapC, mazE-mazF and phd-doc TA systems) survives
CC       antibiotic challenge, suggesting the TA systems are not required to
CC       generate drug-resistant cells. However the mutant is more sensitive to
CC       oxidative and heat stress, and does not survive long term starvation
CC       during aerobic growth on complex medium. There is a difference in the
CC       level of branched-chain amino acids, which may play a role in
CC       monitoring the nutritional supply and physiological state of the cell.
CC       {ECO:0000269|PubMed:22199354}.
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DR   EMBL; CP000480; ABK72269.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37716.1; -; Genomic_DNA.
DR   RefSeq; WP_011727560.1; NZ_SIJM01000042.1.
DR   RefSeq; YP_885668.1; NC_008596.1.
DR   AlphaFoldDB; A0QRY0; -.
DR   SMR; A0QRY0; -.
DR   STRING; 246196.MSMEI_1240; -.
DR   EnsemblBacteria; ABK72269; ABK72269; MSMEG_1278.
DR   EnsemblBacteria; AFP37716; AFP37716; MSMEI_1240.
DR   GeneID; 66732740; -.
DR   KEGG; msg:MSMEI_1240; -.
DR   KEGG; msm:MSMEG_1278; -.
DR   PATRIC; fig|246196.19.peg.1267; -.
DR   eggNOG; COG3654; Bacteria.
DR   OMA; YDTLWLK; -.
DR   OrthoDB; 1838027at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   InterPro; IPR006440; Doc.
DR   InterPro; IPR003812; Fido.
DR   PANTHER; PTHR39426; PTHR39426; 1.
DR   Pfam; PF02661; Fic; 1.
DR   TIGRFAMs; TIGR01550; DOC_P1; 1.
DR   PROSITE; PS51459; FIDO; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Repressor; Toxin-antitoxin system; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..130
FT                   /note="Toxin Doc"
FT                   /id="PRO_0000420846"
FT   DOMAIN          5..126
FT                   /note="Fido"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
SQ   SEQUENCE   130 AA;  13972 MW;  47A3212A5B98137E CRC64;
     MTEYLDREDV LTAGSIAFGG ELKVRDYGLL DAAVARPQAT VYGVDAYPRL WDKAAALLQS
     LARNHALVDG NKRTAWAAAW TFLHINGVQL AADFDVDRAE DLMNEVATRD CDLDSIAAEL
     AGFAAAAQTG