MSAB1_STRPN
ID MSAB1_STRPN Reviewed; 312 AA.
AC P0A3Q9; P35593;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB 1;
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=msrAB1; Synonyms=exp3, msrA; OrderedLocusNames=SP_1359;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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 {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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
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; AE005672; AAK75457.1; -; Genomic_DNA.
DR PIR; H95157; H95157.
DR RefSeq; WP_000818207.1; NZ_AKVY01000001.1.
DR PDB; 3E0M; X-ray; 2.40 A; A/B/C/D=1-312.
DR PDBsum; 3E0M; -.
DR AlphaFoldDB; P0A3Q9; -.
DR SMR; P0A3Q9; -.
DR STRING; 170187.SP_1359; -.
DR EnsemblBacteria; AAK75457; AAK75457; SP_1359.
DR GeneID; 60233101; -.
DR KEGG; spn:SP_1359; -.
DR eggNOG; COG0225; Bacteria.
DR eggNOG; COG0229; Bacteria.
DR OMA; PLRHYVL; -.
DR PhylomeDB; P0A3Q9; -.
DR BioCyc; SPNE170187:G1FZB-1366-MON; -.
DR EvolutionaryTrace; P0A3Q9; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01400; MsrB; 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; Cell membrane; Membrane; Multifunctional enzyme;
KW Oxidoreductase.
FT CHAIN 1..312
FT /note="Peptide methionine sulfoxide reductase MsrA/MsrB 1"
FT /id="PRO_0000138517"
FT DOMAIN 172..295
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 1..155
FT /note="Peptide methionine sulfoxide reductase"
FT ACT_SITE 10
FT /evidence="ECO:0000250"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3E0M"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3E0M"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:3E0M"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:3E0M"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:3E0M"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3E0M"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:3E0M"
FT HELIX 304..309
FT /evidence="ECO:0007829|PDB:3E0M"
SQ 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
