GLPQ_HAEIN
ID GLPQ_HAEIN Reviewed; 364 AA.
AC Q06282;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glycerophosphodiester phosphodiesterase;
DE Short=Glycerophosphoryl diester phosphodiesterase;
DE EC=3.1.4.46;
DE AltName: Full=Immunoglobulin D-binding protein;
DE Short=IgD-binding protein;
DE AltName: Full=Surface-exposed lipoprotein D;
DE Short=Protein D;
DE Flags: Precursor;
GN Name=glpQ; Synonyms=hpd; OrderedLocusNames=HI_0689;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NTHi 772;
RX PubMed=1987023; DOI=10.1128/iai.59.1.119-125.1991;
RA Janson H., Heden L.-O., Grubb A., Ruan M., Forsgren A.;
RT "Protein D, an immunoglobulin D-binding protein of Haemophilus influenzae:
RT cloning, nucleotide sequence, and expression in Escherichia coli.";
RL Infect. Immun. 59:119-125(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Minna / Serotype B;
RX PubMed=8104899; DOI=10.1128/iai.61.11.4546-4552.1993;
RA Janson H., Ruan M., Forsgren A.;
RT "Limited diversity of the protein D gene (hpd) among encapsulated and
RT nonencapsulated Haemophilus influenzae strains.";
RL Infect. Immun. 61:4546-4552(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3639, 3640, 6-7626, Eagan / Serotype B, HK695 / Serotype B, and
RC NCTC 8468 / Serotype B;
RX PubMed=7822043; DOI=10.1128/iai.63.2.696-699.1995;
RA Song X.-M., Forsgren A., Janson H.;
RT "The gene encoding protein D (hpd) is highly conserved among Haemophilus
RT influenzae type b and nontypeable strains.";
RL Infect. Immun. 63:696-699(1995).
RN [5]
RP CHARACTERIZATION, DIACYLGLYCEROL AT CYS-19, AND PALMITOYLATION AT CYS-19.
RC STRAIN=NTHi 772;
RX PubMed=1548059; DOI=10.1128/iai.60.4.1336-1342.1992;
RA Janson H., Heden L.-O., Forsgren A.;
RT "Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae,
RT is a lipoprotein.";
RL Infect. Immun. 60:1336-1342(1992).
CC -!- FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes
CC deacylated phospholipids to G3P and the corresponding alcohols. Has a
CC specific affinity for human immunoglobulin D myeloma protein.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.
CC -!- PTM: Contains both ester- and amide-linked fatty acids.
CC -!- MISCELLANEOUS: The sequence shown is that of strains NTHI 772 and RD /
CC KW20.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; L42023; AAC22348.1; -; Genomic_DNA.
DR EMBL; M37487; AAA24998.1; -; Genomic_DNA.
DR EMBL; L12445; AAA24999.1; -; Genomic_DNA.
DR EMBL; Z35656; CAA84715.1; -; Genomic_DNA.
DR EMBL; Z35657; CAA84716.1; -; Genomic_DNA.
DR EMBL; Z35658; CAA84717.1; -; Genomic_DNA.
DR EMBL; Z35659; CAA84718.1; -; Genomic_DNA.
DR EMBL; Z35660; CAA84719.1; -; Genomic_DNA.
DR EMBL; Z35661; CAA84720.1; -; Genomic_DNA.
DR PIR; G64086; G64086.
DR PIR; S59931; S59931.
DR PIR; S59932; S59932.
DR PIR; S59933; S59933.
DR PIR; S59934; S59934.
DR PIR; S59936; S59936.
DR RefSeq; NP_438849.1; NC_000907.1.
DR RefSeq; WP_005694613.1; NC_000907.1.
DR AlphaFoldDB; Q06282; -.
DR SMR; Q06282; -.
DR STRING; 71421.HI_0689; -.
DR EnsemblBacteria; AAC22348; AAC22348; HI_0689.
DR KEGG; hin:HI_0689; -.
DR PATRIC; fig|71421.8.peg.720; -.
DR eggNOG; COG0584; Bacteria.
DR HOGENOM; CLU_030226_1_0_6; -.
DR OMA; CRHENDI; -.
DR PhylomeDB; Q06282; -.
DR BioCyc; HINF71421:G1GJ1-724-MON; -.
DR BRENDA; 3.1.4.46; 2529.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Calcium; Cell outer membrane; Glycerol metabolism; Hydrolase; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..18
FT CHAIN 19..364
FT /note="Glycerophosphodiester phosphodiesterase"
FT /id="PRO_0000012595"
FT DOMAIN 35..360
FT /note="GP-PDE"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:1548059"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:1548059"
FT VARIANT 13
FT /note="A -> T (in strain: NCTC 8468)"
FT VARIANT 16
FT /note="L -> V (in strain: NCTC 8468)"
FT VARIANT 25
FT /note="N -> S (in strain: NCTC 8468)"
FT VARIANT 28
FT /note="N -> K (in strain: 6-7626)"
FT VARIANT 34
FT /note="D -> H (in strain: NCTC 8468)"
FT VARIANT 62
FT /note="H -> Q (in strain: Eagan, 3639, 3640, 6-7626, HK695
FT and Minna)"
FT VARIANT 63
FT /note="S -> A (in strain: Eagan, 3639, 3640, NCTC 8468, 6-
FT 7626, HK695 and Minna)"
FT VARIANT 98
FT /note="Y -> H (in strain: Eagan, 3639, 3640, NCTC 8468, 6-
FT 7626, HK695 and Minna)"
FT VARIANT 99
FT /note="R -> H (in strain: NCTC 8468)"
FT VARIANT 144
FT /note="K -> Q (in strain: 6-7626)"
FT VARIANT 168
FT /note="K -> R (in strain: 6-7626)"
FT VARIANT 191
FT /note="T -> A (in strain: Eagan, 3639, 3640, NCTC 8468, 6-
FT 7626, HK695 and Minna)"
FT VARIANT 253
FT /note="P -> S (in strain: 6-7626)"
FT VARIANT 310
FT /note="Q -> K (in strain: 6-7626)"
FT VARIANT 327
FT /note="E -> A (in strain: Eagan, 3639, NCTC 8468, 6-7626,
FT HK695 and Minna)"
FT VARIANT 338
FT /note="A -> V (in strain: Eagan, 3640, HK695 and Minna)"
FT VARIANT 364
FT /note="K -> E (in strain: 6-7626)"
SQ SEQUENCE 364 AA; 41902 MW; A6079B3ABF70E820 CRC64;
MKLKTLALSL LAAGVLAGCS SHSSNMANTQ MKSDKIIIAH RGASGYLPEH TLESKALAFA
QHSDYLEQDL AMTKDGRLVV IHDHFLDGLT DVAKKFPYRH RKDGRYYVID FTLKEIQSLE
MTENFETKDG KQAQVYPNRF PLWKSHFRIH TFEDEIEFIQ GLEKSTGKKV GIYPEIKAPW
FHHQNGKDIA TETLKVLKKY GYDKKTDMVY LQTFDFNELK RIKTELLPQM GMDLKLVQLI
AYTDWKETQE KDPKGYWVNY NYDWMFKPGA MAEVVKYADG VGPGWYMLVN KEESKPDNIV
YTPLVKELAQ YNVEVHPYTV RKDALPEFFT DVNQMYDALL NKSGATGVFT DFPDTGVEFL
KGIK