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

Peptide methionine sulfoxide reductase MsrA/MsrB 1 [Includes: Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase); Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase)]

 MSAB1_STRR6             Reviewed;         312 AA.
P0A3R0; P35593;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
28-FEB-2018, entry version 86.
RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB 1;
Includes:
RecName: Full=Peptide methionine sulfoxide reductase MsrA;
Short=Protein-methionine-S-oxide reductase;
EC=1.8.4.11;
AltName: Full=Peptide-methionine (S)-S-oxide reductase;
Short=Peptide Met(O) reductase;
Includes:
RecName: Full=Peptide methionine sulfoxide reductase MsrB;
EC=1.8.4.12;
AltName: Full=Peptide-methionine (R)-S-oxide reductase;
Name=msrAB1; Synonyms=exp3, msrA; OrderedLocusNames=spr1217;
Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=171101;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, POSSIBLE
FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
PubMed=8755589; DOI=10.1073/pnas.93.15.7985;
Wizemann T.M., Moskovitz J., Pearce B.J., Cundell D., Arvidson C.G.,
So M., Weissbach H., Brot N., Masure H.R.;
"Peptide methionine sulfoxide reductase contributes to the maintenance
of adhesins in three major pathogens.";
Proc. Natl. Acad. Sci. U.S.A. 93:7985-7990(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-255 / R6;
PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E.,
LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P.,
McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I.,
Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P.,
Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G.,
Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L.,
Glass J.I.;
"Genome of the bacterium Streptococcus pneumoniae strain R6.";
J. Bacteriol. 183:5709-5717(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-249.
PubMed=7934910; DOI=10.1111/j.1365-2958.1993.tb01233.x;
Pearce B.J., Yin Y.B., Masure H.R.;
"Genetic identification of exported proteins in Streptococcus
pneumoniae.";
Mol. Microbiol. 9:1037-1050(1993).
-!- FUNCTION: Has an important function as a repair enzyme for
proteins that have been inactivated by oxidation (By similarity).
Catalyzes the reversible oxidation-reduction of methionine
sulfoxide in proteins to methionine. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
{ECO:0000269|PubMed:8755589}.
-!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
L-methionine (S)-S-oxide + thioredoxin.
{ECO:0000269|PubMed:8755589}.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
{ECO:0000269|PubMed:8755589}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral
membrane protein {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Mutant exhibits decreased binding to
GalNAcbeta1-4Gal containing receptors that are present on type II
lung cells and vascular endothelial cells.
{ECO:0000269|PubMed:8755589}.
-!- SIMILARITY: In the N-terminal section; belongs to the MsrA Met
sulfoxide reductase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
sulfoxide reductase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U41735; AAC44298.1; -; Genomic_DNA.
EMBL; AE007317; AAL00021.1; -; Genomic_DNA.
PIR; H98023; H98023.
RefSeq; NP_358810.1; NC_003098.1.
RefSeq; WP_000818207.1; NC_003098.1.
ProteinModelPortal; P0A3R0; -.
SMR; P0A3R0; -.
STRING; 171101.spr1217; -.
EnsemblBacteria; AAL00021; AAL00021; spr1217.
GeneID; 934434; -.
KEGG; spr:spr1217; -.
PATRIC; fig|171101.6.peg.1321; -.
eggNOG; ENOG4105E0X; Bacteria.
eggNOG; COG0225; LUCA.
eggNOG; COG0229; LUCA.
HOGENOM; HOG000243423; -.
KO; K12267; -.
OMA; NDAYQPL; -.
BioCyc; SPNE171101:G1FZH-1257-MONOMER; -.
Proteomes; UP000000586; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC.
GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-EC.
GO; GO:0030091; P:protein repair; IEA:InterPro.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
Gene3D; 3.30.1060.10; -; 1.
HAMAP; MF_01401; MsrA; 1.
HAMAP; MF_01400; MsrB; 1.
InterPro; IPR028427; Met_Sox_Rdtase.
InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
InterPro; IPR011057; Mss4-like_sf.
PANTHER; PTHR10173; PTHR10173; 1.
Pfam; PF01625; PMSR; 1.
Pfam; PF01641; SelR; 1.
SUPFAM; SSF51316; SSF51316; 1.
SUPFAM; SSF55068; SSF55068; 1.
TIGRFAMs; TIGR00401; msrA; 1.
TIGRFAMs; TIGR00357; TIGR00357; 1.
PROSITE; PS51790; MSRB; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Membrane; Multifunctional enzyme;
Oxidoreductase; Reference proteome.
CHAIN 1 312 Peptide methionine sulfoxide reductase
MsrA/MsrB 1.
/FTId=PRO_0000138518.
DOMAIN 172 295 MsrB. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
REGION 1 155 Peptide methionine sulfoxide reductase.
ACT_SITE 10 10 {ECO:0000250}.
ACT_SITE 284 284 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
CONFLICT 29 29 V -> G (in Ref. 1; AAC44298).
{ECO:0000305}.
CONFLICT 45 45 K -> E (in Ref. 1; AAC44298).
{ECO:0000305}.
CONFLICT 52 57 TVQVIY -> AVRVIC (in Ref. 1; AAC44298).
{ECO:0000305}.
CONFLICT 61 61 E -> G (in Ref. 1; AAC44298).
{ECO:0000305}.
SEQUENCE 312 AA; 35703 MW; 6F3873FCE9C1F6E1 CRC64;
MAEIYLAGGC FWGLEEYFSR ISGVLETSVG YANGQVETTN YQLLKETDHA ETVQVIYDEK
EVSLREILLY YFRVIDPLSI NQQGNDRGRQ YRTGIYYQDE ADLPAIYTVV QEQERMLGRK
IAVEVEQLRH YILAEDYHQD YLRKNPSGYC HIDVTDADKP LIDAANYEKP SQEVLKASLS
EESYRVTQEA ATEAPFTNAY DQTFEEGIYV DITTGEPLFF AKDKFASGCG WPSFSRPISK
ELIHYYKDLS HGMERIEVRS RSGSAHLGHV FTDGPRELGG LRYCINSASL RFVAKDEMEK
AGYGYLLPYL NK


Related products :

Catalog number Product name Quantity
EIAAB25528 Homo sapiens,Human,Mitochondrial peptide methionine sulfoxide reductase,MSRA,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,PMSR,Protein-methionine-S-oxide reductase
EIAAB25530 Mitochondrial peptide methionine sulfoxide reductase,Mouse,Msra,Mus musculus,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,PMSR,Protein-methionine-S-oxide reductase
EIAAB25529 Mitochondrial peptide methionine sulfoxide reductase,Msra,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,PMSR,Protein-methionine-S-oxide reductase,Rat,Rattus norvegicus
EIAAB25527 Bos taurus,Bovine,Mitochondrial peptide methionine sulfoxide reductase,MSRA,Peptide Met(O) reductase,Peptide-methionine (S)-S-oxide reductase,Protein-methionine-S-oxide reductase
CSB-EL015051RA Rat Mitochondrial peptide methionine sulfoxide reductase(MSRA) ELISA kit 96T
CSB-EL015051MO Mouse Mitochondrial peptide methionine sulfoxide reductase(MSRA) ELISA kit 96T
CSB-EL015051BO Bovine Mitochondrial peptide methionine sulfoxide reductase(MSRA) ELISA kit 96T
CSB-EL015051RA Rat Mitochondrial peptide methionine sulfoxide reductase(MSRA) ELISA kit SpeciesRat 96T
CSB-E17036h Human Mitochondrial peptide methionine sulfoxide reductase (MSRA) ELISA kit 96T
CSB-EL015051MO Mouse Mitochondrial peptide methionine sulfoxide reductase(MSRA) ELISA kit SpeciesMouse 96T
CSB-EL015051BO Bovine Mitochondrial peptide methionine sulfoxide reductase(MSRA) ELISA kit SpeciesBovine 96T
CSB-E17036h Human Mitochondrial peptide methionine sulfoxide reductase (MSRA) ELISA kit SpeciesHuman 96T
LF-MA0083 anti-Methionine Sulfoxide Reductase A , Mouse monoclonal to Methionine Sulfoxide Reductase A, Isotype IgG1, Host Mouse 100 ul
LF-MA0084 anti-Methionine Sulfoxide Reductase A , Mouse monoclonal to Methionine Sulfoxide Reductase A, Isotype IgG2b, Host Mouse 100 ul
E1400m ELISA Kit FOR Mitochondrial peptide methionine sulfoxide reductase; organism: Mouse; gene name: Msra 96T
LF-PA0031 anti-Methionine Sulfoxide Reductase A , Rabbit polyclonal to Methionine Sulfoxide Reductase A , Isotype IgG, Host Rabbit 100 ul
LF-PA10011 anti-Methionine Sulfoxide Reductase A , Mouse polyclonal to Methionine Sulfoxide Reductase A , Isotype , Host Mouse 50 uL
LF-PA10012 anti-Methionine Sulfoxide Reductase A , Rabbit polyclonal to Methionine Sulfoxide Reductase A , Isotype , Host Rabbit 100 ug
LF-PA0088 anti-Methionine sulfoxide reductase B , Rabbit polyclonal to Methionine sulfoxide reductase B , Isotype IgG, Host Rabbit 100 ul
enz-124 Recombinant E.Coli Methionine Sulfoxide Reductase B MSRB 20
enz-124 Recombinant E.Coli Methionine Sulfoxide Reductase B MSRB 5
enz-124 Recombinant E.Coli Methionine Sulfoxide Reductase B MSRB 1mg
CSB-EL015051HU Human Mitochondrial peptide methionine sulfoxide reductase (MSRA) ELISA kit, Species Human, Sample Type serum, plasma 96T
201-20-3518 MSRA{methionine sulfoxide reductase A}rabbit.pAb 0.2ml
enz-129 Recombinant E.Coli Methionine Sulfoxide Reductase A MSRA 50


 

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