MP83_MYCBO
ID MP83_MYCBO Reviewed; 220 AA.
AC P0CAX7; A0A1R3Y2F5; P0A671; P71493; Q10790; X2BM94;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Cell surface glycolipoprotein MPB83;
DE AltName: Full=Lipoprotein p23;
DE Flags: Precursor;
GN Name=mpb83; OrderedLocusNames=BQ2027_MB2898;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCG / Tokyo;
RX PubMed=8633205; DOI=10.1046/j.1365-3083.1996.d01-68.x;
RA Matsuo T., Matsuo H., Ohara N., Matsumoto S., Kitaura H., Mizuno A.,
RA Yamada T.;
RT "Cloning and sequencing of an MPB70 homologue corresponding to MPB83 from
RT Mycobacterium bovis BCG.";
RL Scand. J. Immunol. 43:483-489(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [4]
RP PROTEIN SEQUENCE OF 28-45 AND 48-62, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP MASS SPECTROMETRY, AND MUTAGENESIS OF 48-THR-THR-49.
RC STRAIN=AN-5;
RX PubMed=12517764; DOI=10.1074/jbc.m207959200;
RA Michell S.L., Whelan A.O., Wheeler P.R., Panico M., Easton R.L.,
RA Etienne A.T., Haslam S.M., Dell A., Morris H.R., Reason A.J.,
RA Herrmann J.L., Young D.B., Hewinson R.G.;
RT "The MPB83 antigen from Mycobacterium bovis contains O-linked mannose and
RT (1-->3)-mannobiose moieties.";
RL J. Biol. Chem. 278:16423-16432(2003).
RN [5]
RP FUNCTION, INTERACTION WITH HOST TLR2, AND SUBCELLULAR LOCATION.
RX PubMed=20800577; DOI=10.1016/j.bbrc.2010.08.085;
RA Chambers M.A., Whelan A.O., Spallek R., Singh M., Coddeville B.,
RA Guerardel Y., Elass E.;
RT "Non-acylated Mycobacterium bovis glycoprotein MPB83 binds to TLR1/2 and
RT stimulates production of matrix metalloproteinase 9.";
RL Biochem. Biophys. Res. Commun. 400:403-408(2010).
CC -!- FUNCTION: Induces expression of human (host) matrix metalloproteinase-9
CC (MMP9) in a TLR1/TLR2-dependent fashion; the acylated 20 first mature
CC residues (residues 25-40) induce the most expression, but whole
CC recombinant protein (non-acylated and non-glycosylated), and
CC mannosylated but not acylated protein (residues 26-220) also induce
CC expression (PubMed:20800577). {ECO:0000269|PubMed:20800577}.
CC -!- SUBUNIT: Interacts with host (human) TLR2 (PubMed:20800577).
CC {ECO:0000269|PubMed:20800577}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Secreted, cell wall {ECO:0000250|UniProtKB:P9WNF3}.
CC Secreted {ECO:0000269|PubMed:12517764, ECO:0000269|PubMed:20800577}.
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 (PubMed:12517764). {ECO:0000269|PubMed:12517764}.
CC -!- PTM: When isolated from culture filtrate runs as 25 and 23 kDa
CC proteins; the larger protein is much less abundant, mostly associated
CC with the cell and starts at residue 28, the shorter is more abundant
CC and starts at residue 48 (PubMed:12517764).
CC {ECO:0000269|PubMed:12517764}.
CC -!- MASS SPECTROMETRY: Mass=18048; Mass_error=2; Method=Electrospray;
CC Note=For the shorter more abundant form, is tri-hexosylated.;
CC Evidence={ECO:0000269|PubMed:12517764};
CC -!- MASS SPECTROMETRY: Mass=17560; Mass_error=2; Method=Electrospray;
CC Note=For the shorter more abundant form, chemically deglycosylated.;
CC Evidence={ECO:0000269|PubMed:12517764};
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DR EMBL; D64165; BAA11027.1; -; Genomic_DNA.
DR EMBL; LT708304; SIU01519.1; -; Genomic_DNA.
DR RefSeq; NP_856543.1; NC_002945.3.
DR RefSeq; WP_003414630.1; NC_002945.4.
DR AlphaFoldDB; P0CAX7; -.
DR SMR; P0CAX7; -.
DR iPTMnet; P0CAX7; -.
DR EnsemblBacteria; SIU01519; SIU01519; BQ2027_MB2898.
DR PATRIC; fig|233413.5.peg.3180; -.
DR OMA; ICGGVQT; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.30.180.10; -; 1.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR Pfam; PF02469; Fasciclin; 1.
DR SMART; SM00554; FAS1; 1.
DR SUPFAM; SSF82153; SSF82153; 1.
DR PROSITE; PS50213; FAS1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Direct protein sequencing; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000305"
FT CHAIN 25..220
FT /note="Cell surface glycolipoprotein MPB83"
FT /id="PRO_0000008787"
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:0000305"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CARBOHYD 48
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:12517764"
FT CARBOHYD 49
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:12517764"
FT MUTAGEN 48..49
FT /note="TT->VV: No longer binds concanavalin A upon
FT expression of residues 1-63 in M.smegmatis."
FT /evidence="ECO:0000269|PubMed:12517764"
FT CONFLICT 36
FT /note="S -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
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
