RSHA_MYCTU
ID RSHA_MYCTU Reviewed; 101 AA.
AC P9WJ69; 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 36.
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=Rv3221A;
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 PROTEIN SEQUENCE OF 1-89, COFACTOR, AND INTERACTION WITH SIGH.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22937074; DOI=10.1371/journal.pone.0043676;
RA Kumar S., Badireddy S., Pal K., Sharma S., Arora C., Garg S.K., Alam M.S.,
RA Agrawal P., Anand G.S., Swaminathan K.;
RT "Interaction of Mycobacterium tuberculosis RshA and SigH is mediated by
RT salt bridges.";
RL PLoS ONE 7:E43676-E43676(2012).
RN [3]
RP IDENTIFICATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12368430; DOI=10.1099/00221287-148-10-2967;
RA Camus J.-C., Pryor M.J., Medigue C., Cole S.T.;
RT "Re-annotation of the genome sequence of Mycobacterium tuberculosis
RT H37Rv.";
RL Microbiology 148:2967-2973(2002).
RN [4]
RP FUNCTION AS AN ANTI-SIGMA FACTOR, INTERACTION WITH SIGH, AND INDUCTION.
RX PubMed=14617153; DOI=10.1046/j.1365-2958.2003.03739.x;
RA Song T., Dove S.L., Lee K.H., Husson R.N.;
RT "RshA, an anti-sigma factor that regulates the activity of the
RT mycobacterial stress response sigma factor SigH.";
RL Mol. Microbiol. 50:949-959(2003).
RN [5]
RP FUNCTION AS AN ANTI-SIGMA FACTOR, BINDING AFFINITY, AND SUBUNIT.
RX PubMed=16298337; DOI=10.1016/j.bbrc.2005.11.032;
RA Jeong E.H., Son Y.M., Hah Y.S., Choi Y.J., Lee K.H., Song T., Kim D.R.;
RT "RshA mimetic peptides inhibiting the transcription driven by a
RT Mycobacterium tuberculosis sigma factor SigH.";
RL Biochem. Biophys. Res. Commun. 339:392-398(2006).
RN [6]
RP PHOSPHORYLATION AT THR-94, INTERACTION WITH SIGH, REGULATION, AND
RP MUTAGENESIS OF THR-94.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18728196; DOI=10.1073/pnas.0801143105;
RA Park S.T., Kang C.M., Husson R.N.;
RT "Regulation of the SigH stress response regulon by an essential protein
RT kinase in Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13105-13110(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. {ECO:0000269|PubMed:14617153,
CC ECO:0000269|PubMed:16298337}.
CC -!- COFACTOR:
CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC Evidence={ECO:0000269|PubMed:22937074, ECO:0000305};
CC Note=Binds 1 iron-sulfur cluster per subunit. As the iron-sulfur
CC cluster is unstable, it is not clear from the contradictory
CC experimental evidence whether it is 2Fe-2S, 4Fe-4S or something
CC intermediate. Nor is it clear which other residues besides Cys-53 and
CC Cys-56 are involved in metal binding (PubMed:22937074).
CC {ECO:0000269|PubMed:22937074, ECO:0000305};
CC -!- SUBUNIT: Interacts (affinity=15 nM) 1:1 with cognate sigma factor SigH
CC under reducing conditions; the complex is disrupted under oxiding
CC conditions or as temperatures rise. Binding inhibits the interaction of
CC SigH with the RNA polymerase catalytic core.
CC {ECO:0000269|PubMed:14617153, ECO:0000269|PubMed:16298337,
CC ECO:0000269|PubMed:18728196, ECO:0000269|PubMed:22937074}.
CC -!- INDUCTION: By SigH, part of the sigH-rshA operon.
CC {ECO:0000269|PubMed:14617153}.
CC -!- PTM: Phosphorylated, probably by PknB. Phosphorylation decreases
CC interaction with SigH, leading to increased SigH-mediated
CC transcription. {ECO:0000269|PubMed:18728196}.
CC -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC superfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP46038.1; -; Genomic_DNA.
DR RefSeq; WP_003416891.1; NZ_NVQJ01000003.1.
DR RefSeq; YP_177945.1; NC_000962.3.
DR AlphaFoldDB; P9WJ69; -.
DR SMR; P9WJ69; -.
DR IntAct; P9WJ69; 2.
DR STRING; 83332.Rv3221A; -.
DR iPTMnet; P9WJ69; -.
DR PaxDb; P9WJ69; -.
DR DNASU; 3205091; -.
DR GeneID; 3205091; -.
DR GeneID; 45427215; -.
DR KEGG; mtu:Rv3221A; -.
DR TubercuList; Rv3221A; -.
DR eggNOG; COG5662; Bacteria.
DR OMA; MSCGEPH; -.
DR PhylomeDB; P9WJ69; -.
DR Proteomes; UP000001584; 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 GO; GO:0016989; F:sigma factor antagonist activity; IDA:MTBBASE.
DR GO; GO:0009408; P:response to heat; IDA:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IDA:MTBBASE.
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 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Phosphoprotein; Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..101
FT /note="Anti-sigma factor RshA"
FT /id="PRO_0000423650"
FT REGION 9..15
FT /note="Inhibits SigH sigma factor activity"
FT REGION 28..34
FT /note="Inhibits SigH sigma factor activity"
FT REGION 38..44
FT /note="Inhibits SigH sigma factor activity"
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:0000305"
FT BINDING 56
FT /ligand="iron-sulfur cluster"
FT /ligand_id="ChEBI:CHEBI:30408"
FT /evidence="ECO:0000305"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18728196"
FT MUTAGEN 94
FT /note="T->A: No in vitro phosphorylation by PknB."
FT /evidence="ECO:0000269|PubMed:18728196"
SQ SEQUENCE 101 AA; 11290 MW; 36636191A0D86341 CRC64;
MSENCGPTDA HADHDDSHGG MGCAEVIAEV WTLLDGECTP ETRERLRRHL EACPGCLRHY
GLEERIKALI GTKCRGDRAP EGLRERLRLE IRRTTIIRGG P
