GLPQ_TREPA
ID GLPQ_TREPA Reviewed; 356 AA.
AC O30405;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Glycerophosphodiester phosphodiesterase;
DE Short=Glycerophosphoryl diester phosphodiesterase;
DE Short=Gpd {ECO:0000303|PubMed:9826352};
DE EC=3.1.4.46;
DE Flags: Precursor;
GN Name=glpQ; Synonyms=glp; OrderedLocusNames=TP_0257;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9311129; DOI=10.1111/j.1574-6968.1997.tb12660.x;
RA Stebeck C.E., Shaffer J.M., Arroll T.W., Lukehart S.A., van Voorhis W.C.;
RT "Identification of the Treponema pallidum subsp. pallidum
RT glycerophosphodiester phosphodiesterase homologue.";
RL FEMS Microbiol. Lett. 154:303-310(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9317025; DOI=10.1128/iai.65.10.4179-4189.1997;
RA Shevchenko D.V., Akins D.R., Robinson E.J., Li M., Shevchenko O.V.,
RA Radolf J.D.;
RT "Identification of homologs for thioredoxin, peptidyl prolyl cis-trans
RT isomerase, and glycerophosphodiester phosphodiesterase in outer membrane
RT fractions from Treponema pallidum, the syphilis spirochete.";
RL Infect. Immun. 65:4179-4189(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
RN [4]
RP FUNCTION IN HOST INFECTION, AND BIOTECHNOLOGY.
RC STRAIN=Nichols;
RX PubMed=9826352; DOI=10.1128/iai.66.12.5763-5770.1998;
RA Cameron C.E., Castro C., Lukehart S.A., Van Voorhis W.C.;
RT "Function and protective capacity of Treponema pallidum subsp. pallidum
RT glycerophosphodiester phosphodiesterase.";
RL Infect. Immun. 66:5763-5770(1998).
RN [5]
RP PALMITOYLATION, AND EXPRESSION IN E.COLI.
RC STRAIN=Nichols;
RX PubMed=10225883; DOI=10.1128/iai.67.5.2266-2276.1999;
RA Shevchenko D.V., Sellati T.J., Cox D.L., Shevchenko O.V., Robinson E.J.,
RA Radolf J.D.;
RT "Membrane topology and cellular location of the Treponema pallidum
RT glycerophosphodiester phosphodiesterase (GlpQ) ortholog.";
RL Infect. Immun. 67:2266-2276(1999).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=12904373; DOI=10.1128/jcm.41.8.3668-3674.2003;
RA Van Voorhis W.C., Barrett L.K., Lukehart S.A., Schmidt B., Schriefer M.,
RA Cameron C.E.;
RT "Serodiagnosis of syphilis: antibodies to recombinant Tp0453, Tp92, and Gpd
RT proteins are sensitive and specific indicators of infection by Treponema
RT pallidum.";
RL J. Clin. Microbiol. 41:3668-3674(2003).
RN [7]
RP SUBCELLULAR LOCATION, PALMITOYLATION, AND EXPRESSION IN E.COLI.
RX PubMed=16159783; DOI=10.1128/jb.187.18.6499-6508.2005;
RA Hazlett K.R., Cox D.L., Decaffmeyer M., Bennett M.P., Desrosiers D.C.,
RA La Vake C.J., La Vake M.E., Bourell K.W., Robinson E.J., Brasseur R.,
RA Radolf J.D.;
RT "TP0453, a concealed outer membrane protein of Treponema pallidum, enhances
RT membrane permeability.";
RL J. Bacteriol. 187:6499-6508(2005).
CC -!- FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes
CC deacylated phospholipids to G3P and the corresponding alcohols.
CC {ECO:0000250}.
CC -!- FUNCTION: Binds human IgA, IgD and the Fc portion of IgG but not IgM,
CC which may contribute to evasion of the human immune system.
CC {ECO:0000269|PubMed:9826352}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:83408; EC=3.1.4.46;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:10225883}; Lipid-anchor
CC {ECO:0000305|PubMed:10225883, ECO:0000305|PubMed:16159783}; Periplasmic
CC side {ECO:0000305|PubMed:10225883}. Note=Has also been identified in
CC cell outer membrane, but this may be incorrect (PubMed:9826352,
CC PubMed:9317025). {ECO:0000269|PubMed:9317025,
CC ECO:0000269|PubMed:9826352}.
CC -!- PTM: Palmitoylated upon expression of a fusion protein with first 40
CC residues fused to PhoA in E.coli. {ECO:0000269|PubMed:10225883,
CC ECO:0000269|PubMed:16159783}.
CC -!- BIOTECHNOLOGY: Immunization of rabbits with this protein partially
CC protects against subsequent intradermal challenge, suggesting it may be
CC a viable vaccine candidate (PubMed:9826352). Recognized by sera from
CC 39/43 syphilis patients, it shows promise as a diagnostic antigen
CC (PubMed:12904373). {ECO:0000269|PubMed:12904373,
CC ECO:0000269|PubMed:9826352}.
CC -!- MISCELLANEOUS: The outer membrane of T.pallidum has no
CC lipopolysaccharides, few proteins and is a fluid and very fragile
CC bilayer. Its lack of surface antigenicity is thought to contribute to
CC the ability of the pathogen to evade the human immune system.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AF004286; AAB81591.1; -; Genomic_DNA.
DR EMBL; U95744; AAC08323.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65246.1; -; Genomic_DNA.
DR PIR; F71346; F71346.
DR RefSeq; WP_010881706.1; NC_021490.2.
DR AlphaFoldDB; O30405; -.
DR SMR; O30405; -.
DR IntAct; O30405; 3.
DR STRING; 243276.TPANIC_0257; -.
DR EnsemblBacteria; AAC65246; AAC65246; TP_0257.
DR GeneID; 57878798; -.
DR KEGG; tpa:TP_0257; -.
DR eggNOG; COG0584; Bacteria.
DR HOGENOM; CLU_030226_1_0_12; -.
DR OMA; CRHENDI; -.
DR OrthoDB; 1542724at2; -.
DR BRENDA; 3.1.4.46; 6429.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Glycerol metabolism; Hydrolase;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..356
FT /note="Glycerophosphodiester phosphodiesterase"
FT /id="PRO_0000012596"
FT DOMAIN 25..314
FT /note="GP-PDE"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ 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
