ID   MPT53_MYCBO             Reviewed;         173 AA.
AC   P0A619; A0A1R3Y2I0; Q10804; X2BMA0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Soluble secreted antigen MPT53;
DE   Flags: Precursor;
GN   Name=mpt53; Synonyms=mpb53; OrderedLocusNames=BQ2027_MB2903C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Disulfide oxidoreductase that catalyzes the oxidation of
CC       reduced, unfolded secreted proteins to form disulfide bonds. Despite a
CC       weak homology to thioredoxin this cannot serve as a substrate for
CC       thioredoxin reductase (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU01524.1; -; Genomic_DNA.
DR   RefSeq; NP_856548.1; NC_002945.3.
DR   RefSeq; WP_003414654.1; NC_002945.4.
DR   AlphaFoldDB; P0A619; -.
DR   SMR; P0A619; -.
DR   EnsemblBacteria; SIU01524; SIU01524; BQ2027_MB2903C.
DR   PATRIC; fig|233413.5.peg.3186; -.
DR   OMA; VPWQPAY; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Redox-active center; Secreted; Signal.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000250"
FT   CHAIN           39..173
FT                   /note="Soluble secreted antigen MPT53"
FT                   /id="PRO_0000034291"
FT   DISULFID        73..76
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   173 AA;  18383 MW;  E67C435C368636D9 CRC64;
     MSLRLVSPIK AFADGIVAVA IAVVLMFGLA NTPRAVAADE RLQFTATTLS GAPFDGASLQ
     GKPAVLWFWT PWCPFCNAEA PSLSQVAAAN PAVTFVGIAT RADVGAMQSF VSKYNLNFTN
     LNDADGVIWA RYNVPWQPAF VFYRADGTST FVNNPTAAMS QDELSGRVAA LTS