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Anti-sigma factor RsrA (Regulator of SigR) (Sigma-R anti-sigma factor RsrA)

 RSRA_STRCO              Reviewed;         105 AA.
Q7AKG8; Q9RL96;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
16-MAY-2012, sequence version 1.
16-JAN-2019, entry version 40.
RecName: Full=Anti-sigma factor RsrA;
AltName: Full=Regulator of SigR;
AltName: Full=Sigma-R anti-sigma factor RsrA;
Name=rsrA; OrderedLocusNames=SCO5217;
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces; Streptomyces albidoflavus group.
NCBI_TaxID=100226;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ANTI-SIGMA FACTOR,
INTERACTION WITH SIGR, SUBUNIT, AND POSSIBLE DISULFIDE BONDS.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=10428967; DOI=10.1093/emboj/18.15.4292;
Kang J.G., Paget M.S.B., Seok Y.J., Hahn M.Y., Bae J.B., Hahn J.S.;
"RsrA, an anti-sigma factor regulated by redox change.";
EMBO J. 18:4292-4298(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=12000953; DOI=10.1038/417141a;
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
Hopwood D.A.;
"Complete genome sequence of the model actinomycete Streptomyces
coelicolor A3(2).";
Nature 417:141-147(2002).
[3]
FUNCTION AS A DISULFIDE STRESS SENSOR, COFACTOR, DISRUPTION PHENOTYPE,
AND MUTAGENESIS OF CYS-3; CYS-11; CYS-31; CYS-41; CYS-44; CYS-61 AND
CYS-62.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=11251822; DOI=10.1046/j.1365-2958.2001.02298.x;
Paget M.S., Bae J.B., Hahn M.Y., Li W., Kleanthous C., Roe J.H.,
Buttner M.J.;
"Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a
thiol-disulphide redox switch.";
Mol. Microbiol. 39:1036-1047(2001).
[4]
FUNCTION AS AN ANTI-SIGMA FACTOR, AND INTERACTION WITH SIGR.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=12381317; DOI=10.1016/S0022-2836(02)00948-8;
Li W., Stevenson C.E., Burton N., Jakimowicz P., Paget M.S.,
Buttner M.J., Lawson D.M., Kleanthous C.;
"Identification and structure of the anti-sigma factor-binding domain
of the disulphide-stress regulated sigma factor sigma(R) from
Streptomyces coelicolor.";
J. Mol. Biol. 323:225-236(2002).
[5]
FUNCTION AS AN ANTI-SIGMA FACTOR, INTERACTION WITH SIGR, COFACTOR,
DISULFIDE BOND, AND MASS SPECTROMETRY.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=14529630; DOI=10.1016/j.jmb.2003.08.038;
Li W., Bottrill A.R., Bibb M.J., Buttner M.J., Paget M.S.,
Kleanthous C.;
"The role of zinc in the disulphide stress-regulated anti-sigma factor
RsrA from Streptomyces coelicolor.";
J. Mol. Biol. 333:461-472(2003).
[6]
ZINC-BINDING, AND MUTAGENESIS OF HIS-37.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=16819828; DOI=10.1021/bi060711v;
Zdanowski K., Doughty P., Jakimowicz P., O'Hara L., Buttner M.J.,
Paget M.S., Kleanthous C.;
"Assignment of the zinc ligands in RsrA, a redox-sensing ZAS protein
from Streptomyces coelicolor.";
Biochemistry 45:8294-8300(2006).
[7]
FUNCTION, AND REDUCTION BY MYCOTHIOL.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=18430082; DOI=10.1111/j.1365-2958.2008.06191.x;
Park J.H., Roe J.H.;
"Mycothiol regulates and is regulated by a thiol-specific antisigma
factor RsrA and sigma(R) in Streptomyces coelicolor.";
Mol. Microbiol. 68:861-870(2008).
[8]
MUTAGENESIS OF 33-LYS--LYS-47; HIS-37; PHE-38; GLU-39; GLU-40; CYS-41;
PRO-43; CYS-44; LEU-45 AND GLU-46.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=21685450; DOI=10.1093/nar/gkr477;
Jung Y.G., Cho Y.B., Kim M.S., Yoo J.S., Hong S.H., Roe J.H.;
"Determinants of redox sensitivity in RsrA, a zinc-containing anti-
sigma factor for regulating thiol oxidative stress response.";
Nucleic Acids Res. 39:7586-7597(2011).
-!- FUNCTION: A redox-regulated anti-sigma factor for extracytoplasmic
function (ECF) sigma factor SigR, and a key sensor of disulfide
stress. Holds SigR, its cognate ECF sigma factor, in an inactive
form, inhibiting its sigma activity under reducing but not
oxidizing conditions; oxidation and reduction of the anti-sigma
factor is reversible. Mycothiol (MSH) is competent for reduction
of RsrA, allowing it to bind to SigR. In conjunction with its
cognate sigma factor SigR may sense the intracellular level of
reduced MSH. Probably releases SigR during oxidative stress.
{ECO:0000269|PubMed:10428967, ECO:0000269|PubMed:11251822,
ECO:0000269|PubMed:12381317, ECO:0000269|PubMed:14529630,
ECO:0000269|PubMed:18430082}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:11251822,
ECO:0000269|PubMed:14529630};
Note=Binds 1 Zn(2+) per subunit. Zinc is not required for SigR-
binding, but is required for anti-sigma factor activity. Zinc-
binding renders RsrA relatively resistant to oxidation.
{ECO:0000269|PubMed:11251822, ECO:0000269|PubMed:14529630};
-!- SUBUNIT: Interacts with cognate sigma factor SigR under reducing
but not oxiding conditions. Treatment with the thiol-oxidzing
agent diamide inhibits the interaction, while incubation with
thioredoxin (trxA) stimulates the interaction.
{ECO:0000269|PubMed:10428967, ECO:0000269|PubMed:12381317,
ECO:0000269|PubMed:14529630}.
-!- PTM: Under oxidizing conditions up to 3 disulfide bonds are
formed. A single disulfide bond inhibits binding to SigR. Cys-11
forms a disulfide bond with either Cys-44 (the major bind) or Cys-
41 (a minor bond).
-!- MASS SPECTROMETRY: Mass=12247; Method=SELDI; Range=1-105;
Note=Partially alkylated with iodoacetamide, has 1 disulfide
bond.; Evidence={ECO:0000269|PubMed:14529630};
-!- MASS SPECTROMETRY: Mass=12361; Method=SELDI; Range=1-105;
Note=Full alkylated with iodoacetamide.;
Evidence={ECO:0000269|PubMed:14529630};
-!- DISRUPTION PHENOTYPE: Viable, but defective in sporulation, white
color. Strong induction of disulfide reductase (trxB) and
thioredoxin-2 (trxC) that is not further induced by diamide. Acts
as a SigR constitutive mutant. A double sigR-rsrA mutant
sporulates normally but is more sensitive to diamide.
{ECO:0000269|PubMed:11251822}.
-!- MISCELLANEOUS: A quadruple Cys-3-Ser, Cys-31-Ser, Cys-61-Ala, Cys-
62-Ala mutant has anti-sigma factor activity and is induced by
diamide.
-!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ010320; CAB61633.1; -; Genomic_DNA.
EMBL; AL939122; CAB94602.1; -; Genomic_DNA.
RefSeq; NP_629364.1; NC_003888.3.
RefSeq; WP_003973755.1; NC_003888.3.
PDB; 5FRF; NMR; -; A=1-105.
PDB; 5FRH; NMR; -; A=1-105.
PDBsum; 5FRF; -.
PDBsum; 5FRH; -.
SMR; Q7AKG8; -.
STRING; 100226.SCO5217; -.
EnsemblBacteria; CAB94602; CAB94602; CAB94602.
GeneID; 1100658; -.
KEGG; sco:SCO5217; -.
PATRIC; fig|100226.15.peg.5301; -.
eggNOG; ENOG4105WMN; Bacteria.
eggNOG; ENOG41128S4; LUCA.
HOGENOM; HOG000247360; -.
InParanoid; Q7AKG8; -.
OMA; PCLEKYG; -.
Proteomes; UP000001973; Chromosome.
GO; GO:0016989; F:sigma factor antagonist activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IMP:UniProtKB.
GO; GO:0051776; P:detection of redox state; IMP:UniProtKB.
GO; GO:0051775; P:response to redox state; IDA:UniProtKB.
GO; GO:0043934; P:sporulation; IMP:UniProtKB.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
InterPro; IPR024020; Anit_sigma_mycothiol_RsrA.
InterPro; IPR014295; Anti-sigma.
InterPro; IPR027383; Znf_put.
Pfam; PF13490; zf-HC2; 1.
TIGRFAMs; TIGR02949; anti_SigH_actin; 1.
TIGRFAMs; TIGR03988; antisig_RsrA; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Metal-binding;
Redox-active center; Reference proteome; Sporulation; Transcription;
Transcription regulation; Zinc.
CHAIN 1 105 Anti-sigma factor RsrA.
/FTId=PRO_0000423652.
REGION 33 47 Contributes to redox-sensitivity.
METAL 11 11 Zinc.
METAL 37 37 Zinc; via tele nitrogen. {ECO:0000305}.
METAL 41 41 Zinc.
METAL 44 44 Zinc.
DISULFID 11 44 Or C-11 with C-41 (about 25%).
{ECO:0000269|PubMed:14529630}.
MUTAGEN 3 3 C->S: No effect on sporulation, normal
induction of trxCp1.
{ECO:0000269|PubMed:11251822}.
MUTAGEN 11 11 C->S: No sporulation, constitutive
expression of trxCp1, no binding of SigR.
{ECO:0000269|PubMed:11251822}.
MUTAGEN 31 31 C->S: No effect on sporulation, normal
induction of trxCp1.
{ECO:0000269|PubMed:11251822}.
MUTAGEN 33 47 KFEHHFEECSPCLEK->VLNEHLETCEKCRKH:
Inhibits SigR, no diamide induction. A
swap mutant with RsiW of B.subtilis.
{ECO:0000269|PubMed:21685450}.
MUTAGEN 37 37 H->A: No sporulation, constitutive
disulfide reductase (trxB) activity. No
inhibition of SigR, no diamide induction
of SigR. Binds SigR in vitro.
{ECO:0000269|PubMed:16819828,
ECO:0000269|PubMed:21685450}.
MUTAGEN 38 38 F->A: No inhibition of SigR, no diamide
induction of SigR.
{ECO:0000269|PubMed:21685450}.
MUTAGEN 39 39 E->A: Wild-type inhibition of SigR, more
induction by diamide.
{ECO:0000269|PubMed:21685450}.
MUTAGEN 40 40 E->A: Wild-type inhibition of SigR, more
induction by diamide.
{ECO:0000269|PubMed:21685450}.
MUTAGEN 41 41 C->A: No inhibition of SigR, no diamide
induction of SigR.
{ECO:0000269|PubMed:11251822,
ECO:0000269|PubMed:21685450}.
MUTAGEN 41 41 C->S: No sporulation, constitutive
expression of trxCp1, no binding of SigR.
{ECO:0000269|PubMed:11251822,
ECO:0000269|PubMed:21685450}.
MUTAGEN 43 43 P->A: Decreases basal levels of SigR and
its induction by diamide; may bind it
more tightly.
{ECO:0000269|PubMed:21685450}.
MUTAGEN 44 44 C->A: No inhibition of SigR, no diamide
induction of SigR.
{ECO:0000269|PubMed:11251822,
ECO:0000269|PubMed:21685450}.
MUTAGEN 44 44 C->S: No sporulation, constitutive
expression of trxCp1, no binding of SigR.
{ECO:0000269|PubMed:11251822,
ECO:0000269|PubMed:21685450}.
MUTAGEN 45 45 L->A: Wild-type inhibition of SigR, more
induction by diamide.
{ECO:0000269|PubMed:21685450}.
MUTAGEN 46 46 E->A: Wild-type inhibition of SigR, more
induction by diamide.
{ECO:0000269|PubMed:21685450}.
MUTAGEN 61 61 C->S: No effect on sporulation, normal
induction of trxCp1.
{ECO:0000269|PubMed:11251822}.
MUTAGEN 62 62 C->S: Reduced sporulation, normal
induction of trxCp1, no binding of SigR.
{ECO:0000269|PubMed:11251822}.
HELIX 11 24 {ECO:0000244|PDB:5FRF}.
HELIX 28 31 {ECO:0000244|PDB:5FRF}.
HELIX 35 38 {ECO:0000244|PDB:5FRF}.
HELIX 42 44 {ECO:0000244|PDB:5FRH}.
STRAND 46 49 {ECO:0000244|PDB:5FRF}.
HELIX 51 60 {ECO:0000244|PDB:5FRF}.
STRAND 61 63 {ECO:0000244|PDB:5FRF}.
HELIX 71 75 {ECO:0000244|PDB:5FRF}.
HELIX 77 84 {ECO:0000244|PDB:5FRF}.
TURN 87 89 {ECO:0000244|PDB:5FRF}.
STRAND 91 95 {ECO:0000244|PDB:5FRF}.
SEQUENCE 105 AA; 11681 MW; B89B9BDB8A7AD1B3 CRC64;
MSCGEPHETD CSEILDHLYE FLDKEMPDSD CVKFEHHFEE CSPCLEKYGL EQAVKKLVKR
CCGQDDVPGD LRAKVMGRLD LIRSGQSVPE HDVAAAPSSS APQES


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