Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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.
07-JUN-2017, entry version 37.
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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
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; -.
GeneID; 29659008; -.
KEGG; sco:SCO5217; -.
PATRIC; fig|100226.15.peg.5301; -.
eggNOG; ENOG4105WMN; Bacteria.
eggNOG; ENOG41128S4; LUCA.
HOGENOM; HOG000247360; -.
InParanoid; Q7AKG8; -.
OMA; PCLEKYG; -.
OrthoDB; POG091H09CC; -.
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:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
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.
GO; GO:0006351; P:transcription, DNA-templated; 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


Related products :

Catalog number Product name Quantity
15-288-22217F AP-3 complex subunit sigma-2 - Adapter-related protein complex 3 sigma-2 subunit; Sigma-adaptin 3b; AP-3 complex sigma-3B subunit; Sigma-3B-adaptin Polyclonal 0.1 mg
15-288-22217F AP-3 complex subunit sigma-2 - Adapter-related protein complex 3 sigma-2 subunit; Sigma-adaptin 3b; AP-3 complex sigma-3B subunit; Sigma-3B-adaptin Polyclonal 0.05 mg
10-288-22217F AP-3 complex subunit sigma-2 - Adapter-related protein complex 3 sigma-2 subunit; Sigma-adaptin 3b; AP-3 complex sigma-3B subunit; Sigma-3B-adaptin 0.1 mg
10-288-22217F AP-3 complex subunit sigma-2 - Adapter-related protein complex 3 sigma-2 subunit; Sigma-adaptin 3b; AP-3 complex sigma-3B subunit; Sigma-3B-adaptin 0.05 mg
AB2B201 Polyclonal Antibodies: Anti-RNA polymerase sigma factor RpoE Polyclonal Antibody; Specificity: Anti-RNA polymerase sigma factor RpoE Polyclonal Antibody ; Application: IHC 0.1mg
LF-MA10299 anti-14-3-3 σ (14-3-3 sigma) (3C3), Mouse monoclonal to 14-3-3 σ (14-3-3 sigma), Isotype IgG1, Host Mouse 100 ug
20-272-191004 14 - 3 - 3 sigma - Mouse monoclonal [1.N.6] to 14 - 3 - 3 sigma; Stratifin; Epithelial cell marker protein 1 Monoclonal 0.25 ml
20-272-191003 14 - 3 - 3 sigma - Mouse monoclonal [1.T.28] to 14 - 3 - 3 sigma; Stratifin; Epithelial cell marker protein 1 Monoclonal 0.05 mg
SCH-AHP1050 RABBIT ANTI 14_3_3 SIGMA, Product Type Polyclonal Antibody, Specificity 14_3_3 SIGMA, Target Species Sheep, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications WB, Clone 0.1 ml
AHP1050 RABBIT ANTI 14_3_3 SIGMA, Product Type Polyclonal Antibody, Specificity 14_3_3 SIGMA, Target Species Sheep, Host Rabbit, Format Serum, Isotypes Polyclonal IgG, Applications WB, Clone 0.1 ml
EIAAB38144 Mouse,Mus musculus,Oprs1,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,Sigmar1
EIAAB38145 Oprs1,Rat,Rattus norvegicus,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,Sigmar1
EIAAB38141 Bos taurus,Bovine,OPRS1,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,SIGMAR1
EIAAB38142 AAG8,Aging-associated gene 8 protein,Homo sapiens,hSigmaR1,Human,OPRS1,SIG-1R,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,SIGMAR1,SR31747-binding pro
MCA4035Z MOUSE ANTI HUMAN 14_3_3 SIGMA Azide Free, Product Type Monoclonal Antibody, Specificity 14_3_3 SIGMA, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applications P*, WB, Cl 0.1 mg
E1384146 RNA Polymerase sigma Factor (ECF) ELISA Kit
E1381258 RNA Polymerase sigma Factor (ECF) ELISA Kit 1
E1380079 Guinea pig RNA Polymerase sigma Factor (ECF) ELISA Kit
20-272-190999 14 - 3 - 3 sigma - BSA and Azide free - Mouse monoclonal [1.N.6] to 14 - 3 - 3 sigma - BSA and Azide free; Stratifin; Epithelial cell marker protein 1 Monoclonal 0.05 mg
EIAAB38143 Chicken,Gallus gallus,OPRS1,RCJMB04_7e2,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,SIGMAR1
20-272-190716 RNA polymerase sigma 70 - Mouse monoclonal [2G10] to RNA polymerase sigma 70 Monoclonal 0.05 ml
PAB16007 Rhodopseudomonas palustris<_i> RNA polymerase sigma factor RpoE protein polyclonal antibody 50 ug
15-288-21486 Receptor-type tyrosine-protein phosphatase S - EC 3.1.3.48; R-PTP-S; Protein-tyrosine phosphatase sigma; R-PTP-sigma Polyclonal 0.1 mg
15-288-21486 Receptor-type tyrosine-protein phosphatase S - EC 3.1.3.48; R-PTP-S; Protein-tyrosine phosphatase sigma; R-PTP-sigma Polyclonal 0.05 mg
10-782-55100 Receptor-type tyrosine-protein phosphatase S - EC 3.1.3.48; R-PTP-S; Protein-tyrosine phosphatase sigma; R-PTP-sigma N_A 0.01 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur