ID   RSHA_MYCTO              Reviewed;         101 AA.
AC   P9WJ68; F2GK95; Q6MWZ6; Q8VJ46;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Anti-sigma factor RshA;
DE   AltName: Full=Regulator of SigH;
DE   AltName: Full=Sigma-H anti-sigma factor RshA;
GN   Name=rshA; OrderedLocusNames=MT3318;
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).
RN   [2]
RP   INDUCTION.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12060776; DOI=10.1073/pnas.102055799;
RA   Kaushal D., Schroeder B.G., Tyagi S., Yoshimatsu T., Scott C., Ko C.,
RA   Carpenter L., Mehrotra J., Manabe Y.C., Fleischmann R.D., Bishai W.R.;
RT   "Reduced immunopathology and mortality despite tissue persistence in a
RT   Mycobacterium tuberculosis mutant lacking alternative sigma factor, SigH.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:8330-8335(2002).
CC   -!- FUNCTION: An redox-regulated anti-sigma factor for extracytoplasmic
CC       function (ECF) sigma factor SigH. ECF sigma factors are held in an
CC       inactive form by a cognate anti-sigma factor. RshA and some peptides
CC       derived from it inhibit the sigma factor activity of SigH. Probably
CC       releases SigH during oxidative stress (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 iron-sulfur cluster per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with cognate sigma factor SigH under reducing
CC       conditions. Binding inhibits the interaction of SigH with the RNA
CC       polymerase catalytic core (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated, probably by PknB. Phosphorylation decreases
CC       interaction with SigH, leading to increased SigH-mediated transcription
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC       superfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47660.1; -; Genomic_DNA.
DR   RefSeq; WP_003416891.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJ68; -.
DR   SMR; P9WJ68; -.
DR   EnsemblBacteria; AAK47660; AAK47660; MT3318.
DR   GeneID; 45427215; -.
DR   KEGG; mtc:MT3318; -.
DR   PATRIC; fig|83331.31.peg.3573; -.
DR   HOGENOM; CLU_155928_0_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR024020; Anit_sigma_mycothiol_RsrA.
DR   InterPro; IPR014295; Anti-sigma.
DR   InterPro; IPR027383; Znf_put.
DR   Pfam; PF13490; zf-HC2; 1.
DR   TIGRFAMs; TIGR02949; anti_SigH_actin; 1.
DR   TIGRFAMs; TIGR03988; antisig_RsrA; 1.
PE   2: Evidence at transcript level;
KW   Iron; Iron-sulfur; Metal-binding; Phosphoprotein; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..101
FT                   /note="Anti-sigma factor RshA"
FT                   /id="PRO_0000427882"
FT   REGION          9..15
FT                   /note="Inhibits SigH sigma factor activity"
FT                   /evidence="ECO:0000250"
FT   REGION          28..34
FT                   /note="Inhibits SigH sigma factor activity"
FT                   /evidence="ECO:0000250"
FT   REGION          38..44
FT                   /note="Inhibits SigH sigma factor activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         23
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000255"
FT   BINDING         49
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000255"
FT   BINDING         53
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         94
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   101 AA;  11290 MW;  36636191A0D86341 CRC64;
     MSENCGPTDA HADHDDSHGG MGCAEVIAEV WTLLDGECTP ETRERLRRHL EACPGCLRHY
     GLEERIKALI GTKCRGDRAP EGLRERLRLE IRRTTIIRGG P