(data stored in ACNUC1104 zone)

SWISSPROT: RSRA_STRCO

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

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