ID   IPGD_SHISO              Reviewed;         538 AA.
AC   Q55286;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Inositol phosphate phosphatase IpgD;
DE            EC=3.1.3.78;
DE   AltName: Full=Effector protein IpgD;
DE   AltName: Full=Phosphatidylinositol 4,5-bisphosphate 4-phosphatase;
GN   Name=ipgD;
OS   Shigella sonnei.
OG   Plasmid pINV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HW383;
RA   Arakawa E., Kato J., Ito K., Watanabe H.;
RT   "Comparison and high conservation of nucleotide sequences of spa-mxi
RT   regions between S.sonnei and S.flexneri -- identification of a new gene
RT   coding plausible membrane protein.";
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts phosphatidylinositol 4,5-bisphosphate (PtdIns 4,5-
CC       P2) to PtdIns 5-P. IpgD is injected by Shigella into the host cell and
CC       is required for invasion. The accumulation of PtdIns 5-P causes
CC       membrane ruffling and actin cytoskeleton rearrangements at the entry
CC       site (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:25674,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC         ChEBI:CHEBI:58456; EC=3.1.3.78;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted via the
CC       Mxi-Spa type III secretion system. It is stored in the bacterial
CC       cytoplasm associated with the chaperone IpgE before being secreted in
CC       response to activation of the type III secretion system (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: Contains the consensus sequence Cys-X(5)-Arg characteristic of
CC       Mg-independent phosphatases.
CC   -!- SIMILARITY: Belongs to the phosphatase IpgD/SopB family. {ECO:0000305}.
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DR   EMBL; D50601; BAA09142.1; -; Genomic_DNA.
DR   RefSeq; WP_000548325.1; NZ_UIQD01000016.1.
DR   AlphaFoldDB; Q55286; -.
DR   STRING; 216599.GCA_000283715_05224; -.
DR   OMA; CWNCKSG; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   InterPro; IPR008108; IpgD/SopB.
DR   Pfam; PF05925; IpgD; 1.
DR   PRINTS; PR01734; TYPE3OMBPROT.
PE   3: Inferred from homology;
KW   Hydrolase; Plasmid; Secreted; Virulence.
FT   CHAIN           1..538
FT                   /note="Inositol phosphate phosphatase IpgD"
FT                   /id="PRO_0000220488"
FT   MOTIF           439..445
FT                   /note="CX5R motif"
FT   ACT_SITE        439
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   538 AA;  59971 MW;  6B76E5A3E1522A85 CRC64;
     MHITNLGLHQ VSFQSGDSYK GAEETGKHKG VSVISYQRVK NGERNKGIEA LNRLYLQNQT
     SLTGKSLLFA RDRAEVFYEA IKLAGGDTSK IKAMMERLDT YKLGEVNKRH INELNKVISE
     EIRAQLGIKN KKELQTKIKQ IFTDYLNNKN WGPVNKNISH HGKNYGFQLT PASHMKIGNK
     NIFVKEYNGK GICCASTRES DHIANMWLSK VVDDEGKEIF SGIRHGVISA YGLKKNSSER
     AVAARNKAEE LVSAALYSRP ELLSQALSGK TVDLKIVSTS LLTPTSLTGG EESMLKDQVN
     ALKGLNSKRG EPTKLLIRNS DGLLKEVSVN LKVVTFNFGV NELALKMGLG WRNVDKLNDE
     SICSLLGDNF LKNGVIGGWA AEAIEKNPPC KNDVIYLANQ IKEIINKKLQ KNDNGEPYKL
     SQRMTLLAYT IGAVPCWNCK SGKDRTGMQD AEIKREIIRK HETGQFSQLN SKLSSEEKRL
     FSTILMNSGN MEIQEMNTGV PGNKVMKKLP LSSLELSYSE RIGDSKIWNM VKGYSSFV