CFP32_MYCTU
ID CFP32_MYCTU Reviewed; 261 AA.
AC P9WIR3; 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 40.
DE RecName: Full=Putative glyoxylase CFP32 {ECO:0000305};
DE AltName: Full=27 kDa antigen Cfp30B {ECO:0000305};
GN Name=cfp32 {ECO:0000303|PubMed:14638775};
GN Synonyms=cfp30B {ECO:0000312|EMBL:CAA07636.1},
GN TB27.3 {ECO:0000312|EMBL:CCP43315.1}; OrderedLocusNames=Rv0577;
GN ORFNames=MTV039.15;
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].
RC STRAIN=ATCC 25618 / H37Rv;
RA Oettinger T.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 4-25, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=H37Rv;
RX PubMed=14638775; DOI=10.1128/iai.71.12.6871-6883.2003;
RA Huard R.C., Chitale S., Leung M., Lazzarini L.C., Zhu H., Shashkina E.,
RA Laal S., Conde M.B., Kritski A.L., Belisle J.T., Kreiswirth B.N.,
RA Lapa e Silva J.R., Ho J.L.;
RT "The Mycobacterium tuberculosis complex-restricted gene cfp32 encodes an
RT expressed protein that is detectable in tuberculosis patients and is
RT positively correlated with pulmonary interleukin-10.";
RL Infect. Immun. 71:6871-6883(2003).
RN [4]
RP FUNCTION, AND OVEREXPRESSION.
RC STRAIN=H37Rv;
RX PubMed=20975714; DOI=10.1038/ncomms1060;
RA Pethe K., Sequeira P.C., Agarwalla S., Rhee K., Kuhen K., Phong W.Y.,
RA Patel V., Beer D., Walker J.R., Duraiswamy J., Jiricek J., Keller T.H.,
RA Chatterjee A., Tan M.P., Ujjini M., Rao S.P., Camacho L., Bifani P.,
RA Mak P.A., Ma I., Barnes S.W., Chen Z., Plouffe D., Thayalan P., Ng S.H.,
RA Au M., Lee B.H., Tan B.H., Ravindran S., Nanjundappa M., Lin X., Goh A.,
RA Lakshminarayana S.B., Shoen C., Cynamon M., Kreiswirth B., Dartois V.,
RA Peters E.C., Glynne R., Brenner S., Dick T.;
RT "A chemical genetic screen in Mycobacterium tuberculosis identifies carbon-
RT source-dependent growth inhibitors devoid of in vivo efficacy.";
RL Nat. Commun. 1:57-57(2010).
RN [5]
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 [6]
RP SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=21761124; DOI=10.1007/s12104-011-9322-5;
RA Buchko G.W., Kim H., Myler P.J., Terwilliger T.C., Kim C.Y.;
RT "Chemical shift assignments for Rv0577, a putative glyoxylase associated
RT with virulence from Mycobacterium tuberculosis.";
RL Biomol. NMR. Assign. 6:43-46(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH TLR2.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=22415304; DOI=10.1096/fj.11-199588;
RA Byun E.H., Kim W.S., Kim J.S., Jung I.D., Park Y.M., Kim H.J., Cho S.N.,
RA Shin S.J.;
RT "Mycobacterium tuberculosis Rv0577, a novel TLR2 agonist, induces
RT maturation of dendritic cells and drives Th1 immune response.";
RL FASEB J. 26:2695-2711(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RA Echols N., Flynn E.M., Stephenson S., Ng H.-L., Alber T.;
RT "Crystal structure of the M. tuberculosis kinase inhibitor homolog
RT Rv0577.";
RL Submitted (SEP-2010) to the PDB data bank.
CC -!- FUNCTION: May function as a glyoxylase involved in the methylglyoxal
CC detoxification pathway (PubMed:20975714). Induces maturation of
CC dendritic cells in a TLR2-dependent manner, causing increased
CC expression of cell-surface molecules (CD80, CD86, MHC class I and II)
CC and pro-inflammatory cytokines (TNF-alpha, IL-6, IL-1 beta and IL-
CC 12p70). Acts via both the NF-kappa-B and MAPK signaling pathways.
CC Induces Th1-polarized immune responses (PubMed:22415304).
CC {ECO:0000269|PubMed:20975714, ECO:0000269|PubMed:22415304}.
CC -!- SUBUNIT: Monomer in solution (PubMed:21761124). Interacts with human
CC TLR2 (PubMed:22415304). {ECO:0000269|PubMed:21761124,
CC ECO:0000269|PubMed:22415304}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14638775}.
CC -!- INDUCTION: Expressed in tuberculosis patients.
CC {ECO:0000269|PubMed:14638775}.
CC -!- MISCELLANEOUS: Overexpression confers resistance to pyrimidine-
CC imidazoles (PIs) compounds. {ECO:0000269|PubMed:20975714}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ007737; CAA07636.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43315.1; -; Genomic_DNA.
DR PIR; H70933; H70933.
DR RefSeq; NP_215091.1; NC_000962.3.
DR RefSeq; WP_003403012.1; NZ_NVQJ01000036.1.
DR PDB; 3OXH; X-ray; 1.75 A; A=1-261.
DR PDBsum; 3OXH; -.
DR AlphaFoldDB; P9WIR3; -.
DR BMRB; P9WIR3; -.
DR SMR; P9WIR3; -.
DR STRING; 83332.Rv0577; -.
DR PaxDb; P9WIR3; -.
DR DNASU; 887732; -.
DR GeneID; 887732; -.
DR KEGG; mtu:Rv0577; -.
DR TubercuList; Rv0577; -.
DR eggNOG; COG3324; Bacteria.
DR OMA; TVWTTYL; -.
DR PhylomeDB; P9WIR3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome; Repeat;
KW Secreted; Virulence.
FT CHAIN 1..261
FT /note="Putative glyoxylase CFP32"
FT /id="PRO_0000089565"
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"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:3OXH"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:3OXH"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:3OXH"
FT TURN 91..97
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:3OXH"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:3OXH"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:3OXH"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:3OXH"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:3OXH"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:3OXH"
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
