RSHA_MYCS2
ID RSHA_MYCS2 Reviewed; 101 AA.
AC A0QTP3; Q9XCD7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=MSMEG_1915, MSMEI_1875;
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 [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=10400584; DOI=10.1128/jb.181.14.4266-4274.1999;
RA Fernandes N.D., Wu Q.-L., Kong D., Puyang X., Garg S., Husson R.N.;
RT "A mycobacterial extracytoplasmic sigma factor involved in survival
RT following heat shock and oxidative stress.";
RL J. Bacteriol. 181:4266-4274(1999).
RN [2]
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 [3]
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 [4]
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 [5]
RP PROBABLE INTERACTION WITH SIGH, AND MUTAGENESIS OF CYS-25; CYS-40; CYS-55;
RP CYS-58 AND CYS-76.
RC STRAIN=ATCC 700084 / mc(2)155;
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 [6]
RP POSSIBLE PHOSPHORYLATION, AND REGULATION.
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).
CC -!- FUNCTION: A redox-regulated anti-sigma factor for cognate
CC extracytoplasmic function (ECF) sigma factor SigH. ECF sigma factors
CC are held in an inactive form by an anti-sigma factor (Probable).
CC Overexpression leads to increased susceptibility to diamide.
CC {ECO:0000305}.
CC -!- COFACTOR:
CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC Evidence={ECO:0000305};
CC Note=Binds 1 iron-sulfur cluster per subunit. {ECO:0000305};
CC -!- SUBUNIT: Interacts with cognate ECF RNA polymerase 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 -!- INDUCTION: Induced after heat shock (50 degress Celsius). Part of the
CC sigH-rshA operon. {ECO:0000269|PubMed:10400584}.
CC -!- PTM: Phosphorylated, probably by PknB (Probable). Phosphorylation
CC decreases interaction with SigH, probably leading to increased SigH-
CC mediated transcription. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC superfamily. {ECO:0000305}.
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DR EMBL; AF144091; AAD41811.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK70150.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38347.1; -; Genomic_DNA.
DR RefSeq; WP_011728007.1; NZ_SIJM01000020.1.
DR RefSeq; YP_886281.1; NC_008596.1.
DR AlphaFoldDB; A0QTP3; -.
DR SMR; A0QTP3; -.
DR STRING; 246196.MSMEI_1875; -.
DR EnsemblBacteria; ABK70150; ABK70150; MSMEG_1915.
DR EnsemblBacteria; AFP38347; AFP38347; MSMEI_1875.
DR GeneID; 66733350; -.
DR KEGG; msg:MSMEI_1875; -.
DR KEGG; msm:MSMEG_1915; -.
DR PATRIC; fig|246196.19.peg.1897; -.
DR eggNOG; COG5662; Bacteria.
DR OMA; MSCGEPH; -.
DR OrthoDB; 2036019at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW Iron; Iron-sulfur; Metal-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..101
FT /note="Anti-sigma factor RshA"
FT /id="PRO_0000423651"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25
FT /ligand="iron-sulfur cluster"
FT /ligand_id="ChEBI:CHEBI:30408"
FT /evidence="ECO:0000255"
FT BINDING 51
FT /ligand="iron-sulfur cluster"
FT /ligand_id="ChEBI:CHEBI:30408"
FT /evidence="ECO:0000255"
FT BINDING 55
FT /ligand="iron-sulfur cluster"
FT /ligand_id="ChEBI:CHEBI:30408"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="iron-sulfur cluster"
FT /ligand_id="ChEBI:CHEBI:30408"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MUTAGEN 25
FT /note="C->A: Slightly decreased inhibition of SigH."
FT /evidence="ECO:0000269|PubMed:14617153"
FT MUTAGEN 40
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:14617153"
FT MUTAGEN 55
FT /note="C->A: Decreased inhibition of SigH; reduced
FT interaction with SigH."
FT /evidence="ECO:0000269|PubMed:14617153"
FT MUTAGEN 58
FT /note="C->A: Decreased inhibition of SigH; reduced
FT interaction with SigH."
FT /evidence="ECO:0000269|PubMed:14617153"
FT MUTAGEN 76
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:14617153"
SQ SEQUENCE 101 AA; 11606 MW; 974265FA55D88790 CRC64;
MSETEREDER WTPPIGPIDP EHPECAAVIA EVWTLLDGEC TPETRDKLKQ HLEECPTCLR
HYGIEERVKR LIAAKCSGEK APDSLRERLR IQISRTTIIR G
