ID   PG61_MYCTU              Reviewed;         195 AA.
AC   Q6MWV0; V5QQT3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=PE-PGRS family protein PE_PGRS61 {ECO:0000305};
GN   Name=PE_PGRS61 {ECO:0000312|EMBL:CCP46476.1};
GN   OrderedLocusNames=Rv3653 {ECO:0000312|EMBL:CCP46476.1};
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 [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   [2]
RP   FUNCTION, ACTIVITY REGULATION, INTERACTION WITH TLR2, SUBCELLULAR LOCATION,
RP   AND MUTAGENESIS OF ASN-166 AND GLY-168.
RX   PubMed=27483162; DOI=10.1021/acs.biochem.6b00289;
RA   Yeruva V.C., Kulkarni A., Khandelwal R., Sharma Y., Raghunand T.R.;
RT   "The PE_PGRS proteins of Mycobacterium tuberculosis are Ca(2+) binding
RT   mediators of host-pathogen interaction.";
RL   Biochemistry 55:4675-4687(2016).
CC   -!- FUNCTION: Mediates Ca(2+)-dependent up-regulation of the anti-
CC       inflammatory cytokine IL-10. {ECO:0000269|PubMed:27483162}.
CC   -!- ACTIVITY REGULATION: Binding of Ca(2+) to PE_PGRS61 induces
CC       conformational changes and increases affinity for TLR2.
CC       {ECO:0000269|PubMed:27483162}.
CC   -!- SUBUNIT: Interacts with human TLR2. {ECO:0000269|PubMed:27483162}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:27483162}. Cell surface
CC       {ECO:0000269|PubMed:27483162}.
CC   -!- SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP46476.1; -; Genomic_DNA.
DR   RefSeq; WP_003907101.1; NC_000962.3.
DR   RefSeq; YP_178002.1; NC_000962.3.
DR   AlphaFoldDB; Q6MWV0; -.
DR   PaxDb; Q6MWV0; -.
DR   DNASU; 886259; -.
DR   GeneID; 886259; -.
DR   KEGG; mtu:Rv3653; -.
DR   PATRIC; fig|83332.111.peg.4062; -.
DR   TubercuList; Rv3653; -.
DR   eggNOG; COG0657; Bacteria.
DR   OMA; ANCNWID; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Cell wall; Reference proteome; Secreted.
FT   CHAIN           1..195
FT                   /note="PE-PGRS family protein PE_PGRS61"
FT                   /id="PRO_0000438250"
FT   MUTAGEN         166
FT                   /note="N->A: Decreases Ca(2+) binding affinity."
FT                   /evidence="ECO:0000269|PubMed:27483162"
FT   MUTAGEN         168
FT                   /note="G->S: Decreases Ca(2+) binding affinity."
FT                   /evidence="ECO:0000269|PubMed:27483162"
SQ   SEQUENCE   195 AA;  15819 MW;  E101A15018209164 CRC64;
     MLNAPTQALL GRPLVGNGAN GAPGTGANGG DGGILFGSGG AGGSGAAGMA GGNGGAAGLF
     GNGGAGGAGG SATAGAAGAG GNGGAGGLLF GTAGAGGNGG LSLGLGVAGG AGGAGGSGGS
     DTAGHGGTGG AGGLLFGAGE DGTTPGGNGG AGGVAGLFGD GGNGGNAGVG TPAGNVGAGG
     TGGLLLGQDG MTGLT