PG11_MYCTU
ID PG11_MYCTU Reviewed; 584 AA.
AC Q79FW5; F2GMX9; I6X9Q9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=PE-PGRS family protein PE_PGRS11 {ECO:0000305};
DE AltName: Full=PE-PGRS phosphoglycerate mutase {ECO:0000305};
DE EC=5.4.2.12 {ECO:0000269|PubMed:20558725};
GN Name=PE_PGRS11 {ECO:0000312|EMBL:CCP43500.1};
GN OrderedLocusNames=Rv0754 {ECO:0000312|EMBL:CCP43500.1};
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, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP INTERACTION WITH TLR2, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF
RP ARG-289 AND HIS-290.
RX PubMed=20558725; DOI=10.1074/jbc.m110.135251;
RA Chaturvedi R., Bansal K., Narayana Y., Kapoor N., Sukumar N.,
RA Togarsimalemath S.K., Chandra N., Mishra S., Ajitkumar P., Joshi B.,
RA Katoch V.M., Patil S.A., Balaji K.N.;
RT "The multifunctional PE_PGRS11 protein from Mycobacterium tuberculosis
RT plays a role in regulating resistance to oxidative stress.";
RL J. Biol. Chem. 285:30389-30403(2010).
RN [3]
RP FUNCTION, AND INTERACTION WITH TLR2.
RX PubMed=20176745; DOI=10.4049/jimmunol.0903299;
RA Bansal K., Elluru S.R., Narayana Y., Chaturvedi R., Patil S.A.,
RA Kaveri S.V., Bayry J., Balaji K.N.;
RT "PE_PGRS antigens of Mycobacterium tuberculosis induce maturation and
RT activation of human dendritic cells.";
RL J. Immunol. 184:3495-3504(2010).
CC -!- FUNCTION: Induces maturation and activation of human dendritic cells
CC (DCs), via TLR2-dependent activation of ERK1/2, p38 MAPK, and NF-kappa-
CC B signaling pathways, and enhances the ability of DCs to stimulate
CC CD4(+) T cells. By activating DCs, could potentially contribute to the
CC initiation of innate immune responses during tuberculosis infection and
CC hence regulate the clinical course of tuberculosis (PubMed:20176745).
CC Involved in resistance to oxidative stress, via TLR2-dependent
CC activation of the PI3K-ERK1/2-NF-kappa-B signaling pathway and
CC expression of COX-2 and Bcl2. Also abolishes H(2)O(2)-triggered
CC activation of p38 MAPK (PubMed:20558725). {ECO:0000269|PubMed:20176745,
CC ECO:0000269|PubMed:20558725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000269|PubMed:20558725};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20558725};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.82 mM for 3-phospho-D-glycerate {ECO:0000269|PubMed:20558725};
CC pH dependence:
CC Optimum pH is 7.5. Active between pH 6 and 9.
CC {ECO:0000269|PubMed:20558725};
CC -!- SUBUNIT: Interacts with human TLR2. {ECO:0000269|PubMed:20176745,
CC ECO:0000269|PubMed:20558725}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:20558725}. Cell surface
CC {ECO:0000269|PubMed:20558725}.
CC -!- INDUCTION: Up-regulated under hypoxic conditions.
CC {ECO:0000269|PubMed:20558725}.
CC -!- MISCELLANEOUS: Could be an immunodominant antigen.
CC {ECO:0000269|PubMed:20558725}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the mycobacterial PE
CC family. PGRS subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43500.1; -; Genomic_DNA.
DR RefSeq; WP_003403850.1; NZ_NVQJ01000035.1.
DR RefSeq; YP_177752.1; NC_000962.3.
DR AlphaFoldDB; Q79FW5; -.
DR SMR; Q79FW5; -.
DR STRING; 83332.Rv0754; -.
DR PaxDb; Q79FW5; -.
DR DNASU; 888695; -.
DR GeneID; 888695; -.
DR KEGG; mtu:Rv0754; -.
DR PATRIC; fig|83332.111.peg.836; -.
DR TubercuList; Rv0754; -.
DR eggNOG; COG0406; Bacteria.
DR OMA; ANAQGWI; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:MTBBASE.
DR GO; GO:0006096; P:glycolytic process; IDA:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IDA:MTBBASE.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR000084; PE-PGRS_N.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF00934; PE; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 1: Evidence at protein level;
KW Cell wall; Isomerase; Magnesium; Reference proteome; Secreted;
KW Stress response; Virulence.
FT CHAIN 1..584
FT /note="PE-PGRS family protein PE_PGRS11"
FT /id="PRO_5004287637"
FT DOMAIN 1..92
FT /note="PE"
FT /evidence="ECO:0000255"
FT REGION 384..584
FT /note="Phosphoglycerate mutase"
FT /evidence="ECO:0000305"
FT ACT_SITE 290
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT ACT_SITE 365
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT MUTAGEN 289
FT /note="R->A: Lack of phosphoglycerate mutase activity."
FT /evidence="ECO:0000269|PubMed:20558725"
FT MUTAGEN 290
FT /note="H->A: Lack of phosphoglycerate mutase activity."
FT /evidence="ECO:0000269|PubMed:20558725"
SQ SEQUENCE 584 AA; 56945 MW; AFC78BB7E011D420 CRC64;
MSFVIVARDA LAAAAADLAQ IGSAVNAGNL AAANPTTAVA AAAADEVSAA LAALFGAHAR
EYQAAAAQAA AYHEQFVHRL SAAATSYAVT EVTIATSLRG ALGSAPASVS DGFQAFVYGP
IHATGQQWIN SPVGEALAPI VNAPTNVLLG RDLIGNGVTG TAAAPNGGPG GLLFGDGGAG
YTGGNGGSAG LIGNGGTGGA GFAGGVGGMG GTGGWLMGNG GMGGAGGVGG NGGAGGQALL
FGNGGLGGAG GAGGVDGAIG RGGWFIGTGG MATIGGGGNG QSIVIDFVRH GQTPGNAAML
IDTAVPGPGL TALGQQQAQA IANALAAKGP YAGIFDSQLI RTQQTAAPLA NLLGMAPQVL
PGLNEIHAGI FEDLPQISPA GLLYLVGPIA WTLGFPIVPM LAPGSTDVNG IVFNRAFTGA
VQTIYDASLA NPVVAADGNI TSVAYSSAFT IGVGTMMNVD NPHPLLLLTH PVPNTGAVVV
QGNPEGGWTL VSWDGIPVGP ASLPTALFVD VRELITAPQY AAYDIWESLF TGDPAAVINA
VRDGADEVGA AVVQFPHAVA DDVIDATGHP YLSGLPIGLP SLIP
