MPT51_MYCTU
ID MPT51_MYCTU Reviewed; 299 AA.
AC P9WQN7; L0TFA7; O33176; P0A4V6; Q48923;
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=MPT51/MPB51 antigen;
DE Flags: Precursor;
GN Name=mpt51; Synonyms=fbpC1, fbpD, mpb51; OrderedLocusNames=Rv3803c;
GN ORFNames=MTV026.08c;
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., Andersen P.;
RT "Evidence for the secreted protein MPT51 from Mycobacterium tuberculosis is
RT a T-cell antigen.";
RL Submitted (OCT-1997) 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 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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 27-299, FUNCTION, AND SUBUNIT.
RX PubMed=14672660; DOI=10.1016/j.jmb.2003.11.001;
RA Wilson R.A., Maughan W.N., Kremer L., Besra G.S., Fuetterer K.;
RT "The structure of Mycobacterium tuberculosis MPT51 (FbpC1) defines a new
RT family of non-catalytic alpha/beta hydrolases.";
RL J. Mol. Biol. 335:519-530(2004).
CC -!- FUNCTION: May have a role in host tissue attachment, whereby ligands
CC may include the serum protein fibronectin and small sugars.
CC {ECO:0000269|PubMed:14672660}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14672660}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC {ECO:0000305}.
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DR EMBL; AJ002150; CAA05211.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46632.1; -; Genomic_DNA.
DR PIR; G70887; G70887.
DR RefSeq; WP_003420783.1; NZ_NVQJ01000022.1.
DR RefSeq; YP_178017.1; NC_000962.3.
DR PDB; 1R88; X-ray; 1.71 A; A/B=27-299.
DR PDBsum; 1R88; -.
DR AlphaFoldDB; P9WQN7; -.
DR SMR; P9WQN7; -.
DR STRING; 83332.Rv3803c; -.
DR ESTHER; myctu-mpt51; A85-Mycolyl-transferase.
DR PaxDb; P9WQN7; -.
DR GeneID; 45427804; -.
DR GeneID; 886121; -.
DR KEGG; mtu:Rv3803c; -.
DR TubercuList; Rv3803c; -.
DR eggNOG; COG0627; Bacteria.
DR OMA; VDGNGMW; -.
DR PhylomeDB; P9WQN7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0001968; F:fibronectin binding; IDA:CAFA.
DR GO; GO:0035375; F:zymogen binding; IPI:CAFA.
DR GO; GO:0071769; P:mycolate cell wall layer assembly; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..299
FT /note="MPT51/MPB51 antigen"
FT /id="PRO_0000000230"
FT CONFLICT 246
FT /note="A -> T (in Ref. 1; CAA05211)"
FT /evidence="ECO:0000305"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1R88"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:1R88"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1R88"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1R88"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:1R88"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:1R88"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:1R88"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1R88"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1R88"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:1R88"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:1R88"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1R88"
FT HELIX 280..298
FT /evidence="ECO:0007829|PDB:1R88"
SQ SEQUENCE 299 AA; 31089 MW; 4E2E38F87AEDD73E CRC64;
MKGRSALLRA LWIAALSFGL GGVAVAAEPT AKAAPYENLM VPSPSMGRDI PVAFLAGGPH
AVYLLDAFNA GPDVSNWVTA GNAMNTLAGK GISVVAPAGG AYSMYTNWEQ DGSKQWDTFL
SAELPDWLAA NRGLAPGGHA AVGAAQGGYG AMALAAFHPD RFGFAGSMSG FLYPSNTTTN
GAIAAGMQQF GGVDTNGMWG APQLGRWKWH DPWVHASLLA QNNTRVWVWS PTNPGASDPA
AMIGQAAEAM GNSRMFYNQY RSVGGHNGHF DFPASGDNGW GSWAPQLGAM SGDIVGAIR
