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Glycerophosphodiester phosphodiesterase (Glycerophosphoryl diester phosphodiesterase) (Gpd) (EC 3.1.4.46)

 GLPQ_TREPA              Reviewed;         356 AA.
O30405;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 112.
RecName: Full=Glycerophosphodiester phosphodiesterase;
Short=Glycerophosphoryl diester phosphodiesterase;
Short=Gpd {ECO:0000303|PubMed:9826352};
EC=3.1.4.46;
Flags: Precursor;
Name=glpQ; Synonyms=glp; OrderedLocusNames=TP_0257;
Treponema pallidum (strain Nichols).
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=243276;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Nichols;
PubMed=9311129; DOI=10.1111/j.1574-6968.1997.tb12660.x;
Stebeck C.E., Shaffer J.M., Arroll T.W., Lukehart S.A.,
van Voorhis W.C.;
"Identification of the Treponema pallidum subsp. pallidum
glycerophosphodiester phosphodiesterase homologue.";
FEMS Microbiol. Lett. 154:303-310(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9317025;
Shevchenko D.V., Akins D.R., Robinson E.J., Li M., Shevchenko O.V.,
Radolf J.D.;
"Identification of homologs for thioredoxin, peptidyl prolyl cis-trans
isomerase, and glycerophosphodiester phosphodiesterase in outer
membrane fractions from Treponema pallidum, the syphilis spirochete.";
Infect. Immun. 65:4179-4189(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nichols;
PubMed=9665876; DOI=10.1126/science.281.5375.375;
Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
Weidman J.F., Smith H.O., Venter J.C.;
"Complete genome sequence of Treponema pallidum, the syphilis
spirochete.";
Science 281:375-388(1998).
[4]
FUNCTION IN HOST INFECTION, AND BIOTECHNOLOGY.
STRAIN=Nichols;
PubMed=9826352;
Cameron C.E., Castro C., Lukehart S.A., Van Voorhis W.C.;
"Function and protective capacity of Treponema pallidum subsp.
pallidum glycerophosphodiester phosphodiesterase.";
Infect. Immun. 66:5763-5770(1998).
[5]
PALMITOYLATION, AND EXPRESSION IN E.COLI.
STRAIN=Nichols;
PubMed=10225883;
Shevchenko D.V., Sellati T.J., Cox D.L., Shevchenko O.V.,
Robinson E.J., Radolf J.D.;
"Membrane topology and cellular location of the Treponema pallidum
glycerophosphodiester phosphodiesterase (GlpQ) ortholog.";
Infect. Immun. 67:2266-2276(1999).
[6]
BIOTECHNOLOGY.
PubMed=12904373; DOI=10.1128/JCM.41.8.3668-3674.2003;
Van Voorhis W.C., Barrett L.K., Lukehart S.A., Schmidt B.,
Schriefer M., Cameron C.E.;
"Serodiagnosis of syphilis: antibodies to recombinant Tp0453, Tp92,
and Gpd proteins are sensitive and specific indicators of infection by
Treponema pallidum.";
J. Clin. Microbiol. 41:3668-3674(2003).
[7]
SUBCELLULAR LOCATION, PALMITOYLATION, AND EXPRESSION IN E.COLI.
PubMed=16159783; DOI=10.1128/JB.187.18.6499-6508.2005;
Hazlett K.R., Cox D.L., Decaffmeyer M., Bennett M.P., Desrosiers D.C.,
La Vake C.J., La Vake M.E., Bourell K.W., Robinson E.J., Brasseur R.,
Radolf J.D.;
"TP0453, a concealed outer membrane protein of Treponema pallidum,
enhances membrane permeability.";
J. Bacteriol. 187:6499-6508(2005).
-!- FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes
deacylated phospholipids to G3P and the corresponding alcohols.
{ECO:0000250}.
-!- FUNCTION: Binds human IgA, IgD and the Fc portion of IgG but not
IgM, which may contribute to evasion of the human immune system.
{ECO:0000269|PubMed:9826352}.
-!- CATALYTIC ACTIVITY: A glycerophosphodiester + H(2)O = an alcohol +
sn-glycerol 3-phosphate.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000305|PubMed:10225883}; Lipid-anchor
{ECO:0000305|PubMed:10225883, ECO:0000305|PubMed:16159783};
Periplasmic side {ECO:0000305|PubMed:10225883}. Note=Has also been
identified in cell outer membrane, but this may be incorrect
(PubMed:9826352, PubMed:9317025). {ECO:0000269|PubMed:9317025,
ECO:0000269|PubMed:9826352}.
-!- PTM: Palmitoylated upon expression of a fusion protein with first
40 residues fused to PhoA in E.coli. {ECO:0000269|PubMed:10225883,
ECO:0000269|PubMed:16159783}.
-!- BIOTECHNOLOGY: Immunization of rabbits with this protein partially
protects against subsequent intradermal challenge, suggesting it
may be a viable vaccine candidate (PubMed:9826352). Recognized by
sera from 39/43 syphilis patients, it shows promise as a
diagnostic antigen (PubMed:12904373).
{ECO:0000269|PubMed:12904373, ECO:0000269|PubMed:9826352}.
-!- MISCELLANEOUS: The outer membrane of T.pallidum has no
lipopolysaccharides, few proteins and is a fluid and very fragile
bilayer. Its lack of surface antigenicity is thought to contribute
to the ability of the pathogen to evade the human immune system.
{ECO:0000305}.
-!- SIMILARITY: Belongs to the glycerophosphoryl diester
phosphodiesterase family. {ECO:0000305}.
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EMBL; AF004286; AAB81591.1; -; Genomic_DNA.
EMBL; U95744; AAC08323.1; -; Genomic_DNA.
EMBL; AE000520; AAC65246.1; -; Genomic_DNA.
PIR; F71346; F71346.
RefSeq; WP_010881706.1; NC_021490.2.
ProteinModelPortal; O30405; -.
SMR; O30405; -.
IntAct; O30405; 3.
MINT; MINT-6481004; -.
STRING; 243276.TP0257; -.
EnsemblBacteria; AAC65246; AAC65246; TP_0257.
GeneID; 34331398; -.
KEGG; tpa:TP_0257; -.
eggNOG; ENOG4107YU0; Bacteria.
eggNOG; COG0584; LUCA.
KO; K01126; -.
OMA; GRFYAID; -.
Proteomes; UP000000811; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:UniProtKB-EC.
GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
Gene3D; 3.20.20.190; -; 1.
InterPro; IPR030395; GP_PDE_dom.
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
Pfam; PF03009; GDPD; 1.
SUPFAM; SSF51695; SSF51695; 1.
PROSITE; PS51704; GP_PDE; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome;
Glycerol metabolism; Hydrolase; Lipoprotein; Membrane; Palmitate;
Reference proteome; Signal.
SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 21 356 Glycerophosphodiester phosphodiesterase.
/FTId=PRO_0000012596.
DOMAIN 25 314 GP-PDE.
LIPID 21 21 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
LIPID 21 21 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
SEQUENCE 356 AA; 41014 MW; 7AD414E70A4C799A CRC64;
MRGTYCVTLW GGVFAALVAG CASERMIVAY RGAAGYVPEH TFASKVLAFA QGADYLQQDV
VLSKDNQLIV AQSHILDNMT DVAEKFPRRQ RADGHFYVID FTVEELSLLR ATNSFYTRGK
RHTPVYGQRF PLWKPGFRLH TFEEELQFIR GLEQTTGKKI GIYSEIKVPW FHHQEGKDIA
ALTLALLKKY GYQSRSDLVY VQTYDFNELK RIKRELLPKY EMNVKLIQRV AYTDQRETQE
KDSRGKWINY NYNWMFEPGG MQKIAKYADG VGPDWRMLIE NEWSKVGAVR LSPMVSAIQD
AKLECHVHTV RKETLPSYAR TMDEMFSILF KQTGANVVLT DFPDLGVKFL GKPARY


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