ID   MPT53_MYCTO             Reviewed;         173 AA.
AC   P9WG64; L0TAX0; P0A618; Q10804;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Soluble secreted antigen MPT53;
DE   Flags: Precursor;
GN   Name=mpt53; Synonyms=mpb53; OrderedLocusNames=MT2946;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47271.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK47271.1; ALT_INIT; Genomic_DNA.
DR   PIR; A70924; A70924.
DR   RefSeq; WP_003414654.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WG64; -.
DR   SMR; P9WG64; -.
DR   EnsemblBacteria; AAK47271; AAK47271; MT2946.
DR   KEGG; mtc:MT2946; -.
DR   PATRIC; fig|83331.31.peg.3183; -.
DR   HOGENOM; CLU_042529_13_1_11; -.
DR   Proteomes; UP000001020; 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_0000428416"
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