MPT53_MYCTU
ID MPT53_MYCTU Reviewed; 173 AA.
AC P9WG65; 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 37.
DE RecName: Full=Soluble secreted antigen MPT53;
DE Flags: Precursor;
GN Name=mpt53; Synonyms=mpb53; OrderedLocusNames=Rv2878c;
GN ORFNames=MTCY274.09c;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 39-68.
RX PubMed=10089161; DOI=10.1006/mpat.1998.0267;
RA Wiker H.G., Michell S.L., Hewinson R.G., Spierings E., Nagai S., Harboe M.;
RT "Cloning, expression and significance of MPT53 for identification of
RT secreted proteins of Mycobacterium tuberculosis.";
RL Microb. Pathog. 26:207-219(1999).
RN [2]
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 [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 38-173, AND FUNCTION.
RX PubMed=14597624; DOI=10.1074/jbc.m311833200;
RA Goulding C.W., Apostol M.I., Gleiter S., Parseghian A., Bardwell J.,
RA Gennaro M., Eisenberg D.;
RT "Gram-positive DsbE proteins function differently from Gram-negative DsbE
RT homologs. A structure to function analysis of DsbE from Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 279:3516-3524(2004).
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. {ECO:0000269|PubMed:14597624}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; Y09725; CAA70890.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45680.1; -; Genomic_DNA.
DR PIR; A70924; A70924.
DR RefSeq; NP_217394.1; NC_000962.3.
DR RefSeq; WP_003414654.1; NZ_NVQJ01000006.1.
DR PDB; 1LU4; X-ray; 1.12 A; A=38-173.
DR PDBsum; 1LU4; -.
DR AlphaFoldDB; P9WG65; -.
DR SMR; P9WG65; -.
DR STRING; 83332.Rv2878c; -.
DR PaxDb; P9WG65; -.
DR DNASU; 887184; -.
DR GeneID; 887184; -.
DR KEGG; mtu:Rv2878c; -.
DR TubercuList; Rv2878c; -.
DR eggNOG; COG0526; Bacteria.
DR OMA; VPWQPAY; -.
DR PhylomeDB; P9WG65; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:MTBBASE.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:MTBBASE.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Redox-active center; Reference proteome; Secreted; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000269|PubMed:10089161"
FT CHAIN 39..173
FT /note="Soluble secreted antigen MPT53"
FT /id="PRO_0000034290"
FT DISULFID 73..76
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1LU4"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1LU4"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1LU4"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1LU4"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1LU4"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:1LU4"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1LU4"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:1LU4"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1LU4"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:1LU4"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:1LU4"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1LU4"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1LU4"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:1LU4"
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
