ID   HIGA1_MYCTO             Reviewed;         149 AA.
AC   P9WJA6; L0TB29; P95258; Q7D7P8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Antitoxin HigA1 {ECO:0000305};
GN   Name=higA1 {ECO:0000305}; OrderedLocusNames=MT2005;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Antitoxin component of an atypical, type II toxin-antitoxin
CC       chaperone (TAC) system. Probably neutralizes the toxic effects of
CC       cognate toxin HigB1, which also requires SecB-like chaperone MT2006 (AC
CC       Q7D7P7). Autorepresses its operon (higB1-higA1-MT2006).
CC       {ECO:0000250|UniProtKB:P9WJA7}.
CC   -!- SUBUNIT: Interacts with SecB-like chaperone MT2006.
CC       {ECO:0000250|UniProtKB:P9WJA7}.
CC   -!- INDUCTION: Autorepresses its operon (higB1-higA1-MT2006).
CC       {ECO:0000250|UniProtKB:P9WJA7}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK46277.1; -; Genomic_DNA.
DR   PIR; H70638; H70638.
DR   RefSeq; WP_003409886.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJA6; -.
DR   SMR; P9WJA6; -.
DR   EnsemblBacteria; AAK46277; AAK46277; MT2005.
DR   GeneID; 45425926; -.
DR   KEGG; mtc:MT2005; -.
DR   PATRIC; fig|83331.31.peg.2161; -.
DR   HOGENOM; CLU_137917_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   Pfam; PF01381; HTH_3; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Repressor; Toxin-antitoxin system; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..149
FT                   /note="Antitoxin HigA1"
FT                   /id="PRO_0000427863"
FT   DOMAIN          42..96
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   DNA_BIND        53..72
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
SQ   SEQUENCE   149 AA;  16760 MW;  EBCB6124D6BC7158 CRC64;
     MSIDFPLGDD LAGYIAEAIA ADPSFKGTLE DAEEARRLVD ALIALRKHCQ LSQVEVAKRM
     GVRQPTVSGF EKEPSDPKLS TLQRYARALD ARLRLVLEVP TLREVPTWHR LSSYRGSARD
     HQVRVGADKE ILMQTNWARH ISVRQVEVA