ID   CFP32_MYCTO             Reviewed;         261 AA.
AC   P9WIR2; L0T434; O53774; P0A5N8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Putative glyoxylase CFP32 {ECO:0000305};
DE   AltName: Full=27 kDa antigen Cfp30B {ECO:0000305};
GN   Name=cfp32 {ECO:0000250|UniProtKB:P9WIR3}; Synonyms=cfp30B, TB27.3;
GN   OrderedLocusNames=MT0606;
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: May function as a glyoxylase involved in the methylglyoxal
CC       detoxification pathway. Induces maturation of dendritic cells in a
CC       TLR2-dependent manner, causing increased expression of cell-surface
CC       molecules (CD80, CD86, MHC class I and II) and pro-inflammatory
CC       cytokines (TNF-alpha, IL-6, IL-1 beta and IL-12p70). Acts via both the
CC       NF-kappa-B and MAPK signaling pathways. Induces Th1-polarized immune
CC       responses. {ECO:0000250|UniProtKB:P9WIR3}.
CC   -!- SUBUNIT: Interacts with human TLR2. {ECO:0000250|UniProtKB:P9WIR3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P9WIR3}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44829.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK44829.1; ALT_INIT; Genomic_DNA.
DR   PIR; H70933; H70933.
DR   RefSeq; WP_003403012.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIR2; -.
DR   BMRB; P9WIR2; -.
DR   SMR; P9WIR2; -.
DR   EnsemblBacteria; AAK44829; AAK44829; MT0606.
DR   KEGG; mtc:MT0606; -.
DR   PATRIC; fig|83331.31.peg.637; -.
DR   HOGENOM; CLU_069623_2_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.10.180.10; -; 2.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR041581; Glyoxalase_6.
DR   InterPro; IPR037523; VOC.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   Pfam; PF18029; Glyoxalase_6; 1.
DR   SUPFAM; SSF54593; SSF54593; 2.
DR   PROSITE; PS51819; VOC; 2.
PE   3: Inferred from homology;
KW   Repeat; Secreted.
FT   CHAIN           1..261
FT                   /note="Putative glyoxylase CFP32"
FT                   /id="PRO_0000427960"
FT   DOMAIN          11..129
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          143..257
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   REGION          13..123
FT                   /note="Glyoxalase 1"
FT                   /evidence="ECO:0000305"
FT   REGION          149..252
FT                   /note="Glyoxalase 2"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  27343 MW;  E0182A0B00461C76 CRC64;
     MPKRSEYRQG TPNWVDLQTT DQSAAKKFYT SLFGWGYDDN PVPGGGGVYS MATLNGEAVA
     AIAPMPPGAP EGMPPIWNTY IAVDDVDAVV DKVVPGGGQV MMPAFDIGDA GRMSFITDPT
     GAAVGLWQAN RHIGATLVNE TGTLIWNELL TDKPDLALAF YEAVVGLTHS SMEIAAGQNY
     RVLKAGDAEV GGCMEPPMPG VPNHWHVYFA VDDADATAAK AAAAGGQVIA EPADIPSVGR
     FAVLSDPQGA IFSVLKPAPQ Q