ID   MP83_MYCTO              Reviewed;         220 AA.
AC   P9WNF2; L0TAW5; P0A670; P71493; Q10790;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Cell surface glycolipoprotein MPT83;
DE   AltName: Full=Lipoprotein p23;
DE   Flags: Precursor;
GN   Name=mpt83; OrderedLocusNames=MT2940;
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC       Secreted, cell wall {ECO:0000250|UniProtKB:P9WNF3}. Secreted
CC       {ECO:0000250|UniProtKB:P0CAX7}.
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}.
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DR   EMBL; AE000516; AAK47265.1; -; Genomic_DNA.
DR   PIR; D70923; D70923.
DR   RefSeq; WP_003414630.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNF2; -.
DR   SMR; P9WNF2; -.
DR   EnsemblBacteria; AAK47265; AAK47265; MT2940.
DR   KEGG; mtc:MT2940; -.
DR   PATRIC; fig|83331.31.peg.3176; -.
DR   HOGENOM; CLU_031281_3_0_11; -.
DR   Proteomes; UP000001020; 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   3: Inferred from homology;
KW   Cell membrane; Cell wall; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   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_0000427137"
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