MSRA_MYCTU
ID MSRA_MYCTU Reviewed; 182 AA.
AC P9WJM5; L0T5N9; P0A5L0; P96814;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000255|HAMAP-Rule:MF_01401};
DE Short=Protein-methionine-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE EC=1.8.4.11 {ECO:0000255|HAMAP-Rule:MF_01401};
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE Short=Peptide Met(O) reductase {ECO:0000255|HAMAP-Rule:MF_01401};
GN Name=msrA {ECO:0000255|HAMAP-Rule:MF_01401}; OrderedLocusNames=Rv0137c;
GN ORFNames=MTCI5.11c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:0000255|HAMAP-Rule:MF_01401}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01401};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01401};
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01401}.
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DR EMBL; AL123456; CCP42862.1; -; Genomic_DNA.
DR PIR; D70616; D70616.
DR RefSeq; NP_214651.1; NC_000962.3.
DR RefSeq; WP_003400942.1; NZ_NVQJ01000001.1.
DR PDB; 1NWA; X-ray; 1.50 A; A=1-182.
DR PDBsum; 1NWA; -.
DR AlphaFoldDB; P9WJM5; -.
DR SMR; P9WJM5; -.
DR STRING; 83332.Rv0137c; -.
DR PaxDb; P9WJM5; -.
DR DNASU; 886865; -.
DR GeneID; 45424103; -.
DR GeneID; 886865; -.
DR KEGG; mtu:Rv0137c; -.
DR TubercuList; Rv0137c; -.
DR eggNOG; COG0225; Bacteria.
DR OMA; GYCAFVV; -.
DR PhylomeDB; P9WJM5; -.
DR BRENDA; 1.8.4.11; 3445.
DR Reactome; R-HSA-1222538; Tolerance by Mtb to nitric oxide produced by macrophages.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IDA:MTBBASE.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IDA:MTBBASE.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0051409; P:response to nitrosative stress; IMP:MTBBASE.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
DR GO; GO:0052163; P:symbiont defense to host-produced nitric oxide; TAS:Reactome.
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 Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome.
FT CHAIN 1..182
FT /note="Peptide methionine sulfoxide reductase MsrA"
FT /id="PRO_0000138560"
FT ACT_SITE 13
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:1NWA"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:1NWA"
FT STRAND 27..38
FT /evidence="ECO:0007829|PDB:1NWA"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1NWA"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1NWA"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:1NWA"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1NWA"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1NWA"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1NWA"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:1NWA"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1NWA"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1NWA"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1NWA"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1NWA"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1NWA"
SQ SEQUENCE 182 AA; 20485 MW; B0A2847A699C2016 CRC64;
MTSNQKAILA GGCFWGLQDL IRNQPGVVST RVGYSGGNIP NATYRNHGTH AEAVEIIFDP
TVTDYRTLLE FFFQIHDPTT KDRQGNDRGT SYRSAIFYFD EQQKRIALDT IADVEASGLW
PGKVVTEVSP AGDFWEAEPE HQDYLQRYPN GYTCHFVRPG WRLPRRTAES ALRASLSPEL
GT
