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PE-PGRS family protein PE_PGRS11 (PE-PGRS phosphoglycerate mutase) (EC 5.4.2.12)

 PG11_MYCTU              Reviewed;         584 AA.
Q79FW5; F2GMX9; I6X9Q9;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
07-JUN-2017, entry version 81.
RecName: Full=PE-PGRS family protein PE_PGRS11 {ECO:0000305};
AltName: Full=PE-PGRS phosphoglycerate mutase {ECO:0000305};
EC=5.4.2.12 {ECO:0000269|PubMed:20558725};
Name=PE_PGRS11 {ECO:0000312|EMBL:CCP43500.1};
OrderedLocusNames=Rv0754 {ECO:0000312|EMBL:CCP43500.1};
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
INTERACTION WITH TLR2, SUBCELLULAR LOCATION, INDUCTION, AND
MUTAGENESIS OF ARG-289 AND HIS-290.
PubMed=20558725; DOI=10.1074/jbc.M110.135251;
Chaturvedi R., Bansal K., Narayana Y., Kapoor N., Sukumar N.,
Togarsimalemath S.K., Chandra N., Mishra S., Ajitkumar P., Joshi B.,
Katoch V.M., Patil S.A., Balaji K.N.;
"The multifunctional PE_PGRS11 protein from Mycobacterium tuberculosis
plays a role in regulating resistance to oxidative stress.";
J. Biol. Chem. 285:30389-30403(2010).
[3]
FUNCTION, AND INTERACTION WITH TLR2.
PubMed=20176745; DOI=10.4049/jimmunol.0903299;
Bansal K., Elluru S.R., Narayana Y., Chaturvedi R., Patil S.A.,
Kaveri S.V., Bayry J., Balaji K.N.;
"PE_PGRS antigens of Mycobacterium tuberculosis induce maturation and
activation of human dendritic cells.";
J. Immunol. 184:3495-3504(2010).
-!- FUNCTION: Induces maturation and activation of human dendritic
cells (DCs), via TLR2-dependent activation of ERK1/2, p38 MAPK,
and NF-kappa-B signaling pathways, and enhances the ability of DCs
to stimulate CD4(+) T cells. By activating DCs, could potentially
contribute to the initiation of innate immune responses during
tuberculosis infection and hence regulate the clinical course of
tuberculosis (PubMed:20176745). Involved in resistance to
oxidative stress, via TLR2-dependent activation of the PI3K-
ERK1/2-NF-kappa-B signaling pathway and expression of COX-2 and
Bcl2. Also abolishes H(2)O(2)-triggered activation of p38 MAPK
(PubMed:20558725). {ECO:0000269|PubMed:20176745,
ECO:0000269|PubMed:20558725}.
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
{ECO:0000269|PubMed:20558725}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:20558725};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.82 mM for 3-phospho-D-glycerate
{ECO:0000269|PubMed:20558725};
pH dependence:
Optimum pH is 7.5. Active between pH 6 and 9.
{ECO:0000269|PubMed:20558725};
-!- SUBUNIT: Interacts with human TLR2. {ECO:0000269|PubMed:20176745,
ECO:0000269|PubMed:20558725}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:20558725}. Cell surface
{ECO:0000269|PubMed:20558725}.
-!- INDUCTION: Up-regulated under hypoxic conditions.
{ECO:0000269|PubMed:20558725}.
-!- MISCELLANEOUS: Could be an immunodominant antigen.
{ECO:0000269|PubMed:20558725}.
-!- SIMILARITY: In the N-terminal section; belongs to the
mycobacterial PE family. PGRS subfamily. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
phosphoglycerate mutase family. {ECO:0000305}.
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EMBL; AL123456; CCP43500.1; -; Genomic_DNA.
RefSeq; WP_003403850.1; NZ_KK339370.1.
RefSeq; YP_177752.1; NC_000962.3.
ProteinModelPortal; Q79FW5; -.
STRING; 83332.Rv0754; -.
PaxDb; Q79FW5; -.
EnsemblBacteria; CCP43500; CCP43500; Rv0754.
GeneID; 888695; -.
KEGG; mtu:Rv0754; -.
KEGG; mtv:RVBD_0754; -.
PATRIC; fig|83332.111.peg.836; -.
TubercuList; Rv0754; -.
eggNOG; ENOG4105GCF; Bacteria.
eggNOG; COG0406; LUCA.
HOGENOM; HOG000220355; -.
OMA; QAWISSP; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:MTBBASE.
GO; GO:0006096; P:glycolytic process; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0001666; P:response to hypoxia; IDA:MTBBASE.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR013078; His_Pase_superF_clade-1.
InterPro; IPR029033; His_PPase_superfam.
InterPro; IPR000084; PE-PGRS_N.
Pfam; PF00300; His_Phos_1; 1.
Pfam; PF00934; PE; 1.
SMART; SM00855; PGAM; 1.
SUPFAM; SSF53254; SSF53254; 1.
1: Evidence at protein level;
Cell wall; Complete proteome; Isomerase; Magnesium;
Reference proteome; Secreted; Stress response; Virulence.
CHAIN 1 584 PE-PGRS family protein PE_PGRS11.
/FTId=PRO_5004287637.
DOMAIN 1 92 PE. {ECO:0000255}.
REGION 384 584 Phosphoglycerate mutase. {ECO:0000305}.
COMPBIAS 150 280 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
ACT_SITE 290 290 Tele-phosphohistidine intermediate.
{ECO:0000250|UniProtKB:P62707}.
ACT_SITE 365 365 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P62707}.
MUTAGEN 289 289 R->A: Lack of phosphoglycerate mutase
activity. {ECO:0000269|PubMed:20558725}.
MUTAGEN 290 290 H->A: Lack of phosphoglycerate mutase
activity. {ECO:0000269|PubMed:20558725}.
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


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