ID MP83_MYCTU Reviewed; 220 AA.
AC P9WNF3; L0TAW5; P0A670; P71493; Q10790;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Cell surface glycolipoprotein MPT83;
DE AltName: Full=Lipoprotein p23;
DE Flags: Precursor;
GN Name=mpt83; OrderedLocusNames=Rv2873; ORFNames=MTCY274.04;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=8633206; DOI=10.1046/j.1365-3083.1996.d01-78.x;
RA Hewinson R.G., Michell S., Russell W.P., McAdam R.A., Jacobs W.R. Jr.;
RT "Molecular characterization of MPT83: a seroreactive antigen of
RT Mycobacterium tuberculosis with homology to MPT70.";
RL Scand. J. Immunol. 43:490-499(1996).
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.m111.011445;
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 FUNCTION, AND INTERACTION WITH HOST TLR2.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22174456; DOI=10.4049/jimmunol.1102177;
RA Chen S.T., Li J.Y., Zhang Y., Gao X., Cai H.;
RT "Recombinant MPT83 derived from Mycobacterium tuberculosis induces cytokine
RT production and upregulates the function of mouse macrophages through
RT TLR2.";
RL J. Immunol. 188:668-677(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22567094; DOI=10.1371/journal.pone.0034991;
RA Kao F.F., Mahmuda S., Pinto R., Triccas J.A., West N.P., Britton W.J.;
RT "The secreted lipoprotein, MPT83, of Mycobacterium tuberculosis is
RT recognized during human tuberculosis and stimulates protective immunity in
RT mice.";
RL PLoS ONE 7:E34991-E34991(2012).
CC -!- FUNCTION: Recombinant, non-modified protein stimulates secretion of
CC cytokines (TNF-alpha, IL-6 and IL-12p40) by mouse macrophage cell lines
CC in a TLR2-dependent fashion, which leads to increased host innate
CC immunity responses against the bacterium (PubMed:22174456). Serves as a
CC strong human and mouse antigen T cell antigen during M.tuberculosis
CC infection, inducing strong IFN-gamma expression (PubMed:22567094).
CC {ECO:0000269|PubMed:22174456, ECO:0000269|PubMed:22567094}.
CC -!- SUBUNIT: Interacts with host TLR2 (tested in mouse) (PubMed:22174456).
CC {ECO:0000269|PubMed:22174456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000305|PubMed:22567094,
CC ECO:0000305|PubMed:8633206}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}. Secreted, cell wall {ECO:0000305|PubMed:22567094}.
CC Secreted {ECO:0000250|UniProtKB:P0CAX7}.
CC -!- INDUCTION: Highly expressed and immunogenic during infection of mice
CC with live bacteria (at protein level). {ECO:0000269|PubMed:8633206}.
CC -!- PTM: O-glycosylated. Contains 0-3 mannose residues attached to residues
CC 48-49 in various configurations; the dominant glycoform is Thr-
CC 48(Man)/Thr-49(Man2) with an unusual Man(1->3)Man linkage, but
CC Thr48(Man3)/Thr49(Man0) through to Thr48(Man0/)Thr49(Man3) are also
CC seen (By similarity). {ECO:0000250|UniProtKB:P0CAX7}.
CC -!- BIOTECHNOLOGY: Could be used in vaccine production; both recombinant
CC protein and DNA vaccines stimulate antigen-specific T cell responses in
CC mice (PubMed:22567094). {ECO:0000269|PubMed:22567094}.
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DR EMBL; X94597; CAA64290.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45675.1; -; Genomic_DNA.
DR PIR; D70923; D70923.
DR RefSeq; NP_217389.1; NC_000962.3.
DR RefSeq; WP_003414630.1; NZ_NVQJ01000006.1.
DR AlphaFoldDB; P9WNF3; -.
DR SMR; P9WNF3; -.
DR STRING; 83332.Rv2873; -.
DR GlyCosmos; P9WNF3; 2 sites, No reported glycans.
DR PaxDb; 83332-Rv2873; -.
DR DNASU; 887155; -.
DR GeneID; 887155; -.
DR KEGG; mtu:Rv2873; -.
DR TubercuList; Rv2873; -.
DR eggNOG; COG2335; Bacteria.
DR InParanoid; P9WNF3; -.
DR OrthoDB; 9800666at2; -.
DR PhylomeDB; P9WNF3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
DR Gene3D; 2.30.180.10; FAS1 domain; 1.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR PANTHER; PTHR10900:SF77; FI19380P1; 1.
DR PANTHER; PTHR10900; PERIOSTIN-RELATED; 1.
DR Pfam; PF02469; Fasciclin; 1.
DR SMART; SM00554; FAS1; 1.
DR SUPFAM; SSF82153; FAS1 domain; 1.
DR PROSITE; PS50213; FAS1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 25..220
FT /note="Cell surface glycolipoprotein MPT83"
FT /id="PRO_0000008788"
FT DOMAIN 83..215
FT /note="FAS1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CARBOHYD 48
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P0CAX7"
FT CARBOHYD 49
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P0CAX7"
SQ SEQUENCE 220 AA; 22070 MW; 5CB99A4B51852A98 CRC64;
MINVQAKPAA AASLAAIAIA FLAGCSSTKP VSQDTSPKPA TSPAAPVTTA AMADPAADLI
GRGCAQYAAQ NPTGPGSVAG MAQDPVATAA SNNPMLSTLT SALSGKLNPD VNLVDTLNGG
EYTVFAPTNA AFDKLPAATI DQLKTDAKLL SSILTYHVIA GQASPSRIDG THQTLQGADL
TVIGARDDLM VNNAGLVCGG VHTANATVYM IDTVLMPPAQ
//
