MSRAB_HELPY
ID MSRAB_HELPY Reviewed; 359 AA.
AC O25011; O85224;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB;
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA;
DE Short=Protein-methionine-S-oxide reductase;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase MsrB;
DE EC=1.8.4.12;
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase;
GN Name=msrAB; Synonyms=msrA; OrderedLocusNames=HP_0224;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49503 / 60190;
RX PubMed=9596777; DOI=10.1128/iai.66.6.2984-2986.1998;
RA Cao P., McClain M.S., Forsyth M.H., Cover T.L.;
RT "Extracellular release of antigenic proteins by Helicobacter pylori.";
RL Infect. Immun. 66:2984-2986(1998).
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation. Catalyzes the reversible
CC oxidation-reduction of methionine sulfoxide in proteins to methionine
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:50058; EC=1.8.4.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58772; EC=1.8.4.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:50058; EC=1.8.4.12;
CC -!- SIMILARITY: In the N-terminal section; belongs to the MsrA Met
CC sulfoxide reductase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
CC sulfoxide reductase family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07291.1; -; Genomic_DNA.
DR EMBL; AF053709; AAC24211.1; -; Genomic_DNA.
DR PIR; H64547; H64547.
DR RefSeq; NP_207022.1; NC_000915.1.
DR RefSeq; WP_000866624.1; NC_018939.1.
DR PDB; 7E43; X-ray; 2.20 A; A/B=1-359.
DR PDBsum; 7E43; -.
DR AlphaFoldDB; O25011; -.
DR SMR; O25011; -.
DR DIP; DIP-3282N; -.
DR IntAct; O25011; 9.
DR MINT; O25011; -.
DR STRING; 85962.C694_01130; -.
DR PaxDb; O25011; -.
DR EnsemblBacteria; AAD07291; AAD07291; HP_0224.
DR KEGG; hpy:HP_0224; -.
DR PATRIC; fig|85962.47.peg.242; -.
DR eggNOG; COG0225; Bacteria.
DR eggNOG; COG0229; Bacteria.
DR OMA; GEFIPYI; -.
DR PhylomeDB; O25011; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01625; PMSR; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Multifunctional enzyme; Oxidoreductase; Reference proteome.
FT CHAIN 1..359
FT /note="Peptide methionine sulfoxide reductase MsrA/MsrB"
FT /id="PRO_0000138515"
FT DOMAIN 206..329
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 36..189
FT /note="Peptide methionine sulfoxide reductase A"
FT ACT_SITE 44
FT /evidence="ECO:0000250"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT CONFLICT 9
FT /note="N -> I (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="A -> L (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="S -> N (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="A -> T (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="H -> N (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="E -> K (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> G (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="D -> S (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="K -> R (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="N -> Q (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="S -> T (in Ref. 2; AAC24211)"
FT /evidence="ECO:0000305"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:7E43"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 136..151
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:7E43"
FT TURN 170..174
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:7E43"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 272..282
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:7E43"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:7E43"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:7E43"
FT TURN 332..336
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:7E43"
FT HELIX 341..354
FT /evidence="ECO:0007829|PDB:7E43"
SQ SEQUENCE 359 AA; 41275 MW; D481FAC5C60927B3 CRC64;
MKVLSYLKNF YLFLAIGAIM QASENMGSQH QKTDERVIYL AGGCFWGLEA YMERIYGVID
ASSGYANGKT SSTNYEKLHE SDHAESVKVI YDPKKISLDK LLRYYFKVVD PVSVNKQGND
VGRQYRTGIY YVNSADKEVI DHALKALQKE VKGKIAIEVE PLKNYVRAEE YHQDYLKKHP
SGYCHIDLKK ADEVIVDDDK YTKPSDEVLK KKLTKLQYEV TQNKHTEKPF ENEYYNKEEE
GIYVDITTGE PLFSSADKYD SGCGWPSFSK PINKDVVKYE DDESLNRKRI EVLSRIGKAH
LGHVFNDGPK ELGGLRYCIN SAALRFIPLK DMEKEGYGEF IPYIKKGELK KYINDKKSH
