IPGD_SHIFL
ID IPGD_SHIFL Reviewed; 538 AA.
AC Q07566; Q6XVY4; Q8VSH4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
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; OrderedLocusNames=CP0133;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pCP301, and Plasmid pINV_F6_M1382.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=8478058; DOI=10.1128/iai.61.5.1707-1714.1993;
RA Allaoui A., Menard R., Sansonetti P.J., Parsot C.;
RT "Characterization of the Shigella flexneri ipgD and ipgF genes, which are
RT located in the proximal part of the mxi locus.";
RL Infect. Immun. 61:1707-1714(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11115111; DOI=10.1046/j.1365-2958.2000.02179.x;
RA Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H.,
RA Kunst F., Sansonetti P.J., Parsot C.;
RT "The virulence plasmid pWR100 and the repertoire of proteins secreted by
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 38:760-771(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11292750; DOI=10.1128/iai.69.5.3271-3285.2001;
RA Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V.,
RA Blattner F.R.;
RT "Complete DNA sequence and analysis of the large virulence plasmid of
RT Shigella flexneri.";
RL Infect. Immun. 69:3271-3285(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M1382 / Serotype 6; PLASMID=pINV_F6_M1382;
RX PubMed=14573649; DOI=10.1128/iai.71.11.6298-6306.2003;
RA Lan R., Stevenson G., Reeves P.R.;
RT "Comparison of two major forms of the Shigella virulence plasmid pINV:
RT positive selection is a major force driving the divergence.";
RL Infect. Immun. 71:6298-6306(2003).
RN [6]
RP FUNCTION, INTERACTION WITH IPAA, AND SUBCELLULAR LOCATION.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=11029686; DOI=10.1046/j.1365-2958.2000.02041.x;
RA Niebuhr K., Jouihri N., Allaoui A., Gounon P., Sansonetti P.J., Parsot C.;
RT "IpgD, a protein secreted by the type III secretion machinery of Shigella
RT flexneri, is chaperoned by IpgE and implicated in entry focus formation.";
RL Mol. Microbiol. 38:8-19(2000).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF CYS-439.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=12356723; DOI=10.1093/emboj/cdf522;
RA Niebuhr K., Giuriato S., Pedron T., Philpott D.J., Gaits F., Sable J.,
RA Sheetz M.P., Parsot C., Sansonetti P.J., Payrastre B.;
RT "Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S.flexneri effector
RT IpgD reorganizes host cell morphology.";
RL EMBO J. 21:5069-5078(2002).
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. Acts in concert with IpaA to coordinate and control the membrane
CC and cytoskeletal rearrangements induced early after invasion of the
CC host cell. {ECO:0000269|PubMed:11029686, ECO:0000269|PubMed:12356723}.
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:0000269|PubMed:11029686,
CC ECO:0000269|PubMed:8478058}. Note=Secreted via the Mxi-Spa type III
CC secretion system. It is stored in the bacterial cytoplasm associated
CC with the chaperone IpgE before being secreted in response to activation
CC of the type III secretion system.
CC -!- INDUCTION: By growth at 37 degrees Celsius.
CC {ECO:0000269|PubMed:8478058}.
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; L04309; AAA26517.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05808.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18452.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72339.1; -; Genomic_DNA.
DR EMBL; AY206439; AAP78996.1; -; Genomic_DNA.
DR RefSeq; NP_085296.1; NC_002698.1.
DR RefSeq; NP_858266.1; NC_004851.1.
DR RefSeq; WP_010921667.1; NZ_QWST01000007.1.
DR RefSeq; YP_009062490.1; NC_024996.1.
DR AlphaFoldDB; Q07566; -.
DR STRING; 198214.CP0133; -.
DR PRIDE; Q07566; -.
DR EnsemblBacteria; AAL72339; AAL72339; SF_p0133.
DR GeneID; 1238042; -.
DR KEGG; sfl:CP0133; -.
DR PATRIC; fig|198214.7.peg.5387; -.
DR HOGENOM; CLU_025781_1_0_6; -.
DR BioCyc; MetaCyc:MON-14263; -.
DR BRENDA; 3.1.3.78; 5712.
DR Proteomes; UP000001006; Plasmid pCP301.
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 1: Evidence at protein level;
KW Hydrolase; Plasmid; Reference proteome; Secreted; Virulence.
FT CHAIN 1..538
FT /note="Inositol phosphate phosphatase IpgD"
FT /id="PRO_0000220487"
FT MOTIF 439..445
FT /note="CX5R motif"
FT ACT_SITE 439
FT /evidence="ECO:0000255"
FT VARIANT 27..28
FT /note="KH -> NQ (in plasmid pINV_F6_M1382)"
FT VARIANT 48
FT /note="I -> V (in plasmid pINV_F6_M1382)"
FT VARIANT 66
FT /note="S -> G (in plasmid pINV_F6_M1382)"
FT VARIANT 73..78
FT /note="KAEVFC -> RAAVFY (in plasmid pINV_F6_M1382)"
FT VARIANT 73
FT /note="K -> R (in plasmid pCP301)"
FT VARIANT 97
FT /note="R -> Q (in plasmid pINV_F6_M1382)"
FT VARIANT 107
FT /note="N -> D (in plasmid pINV_F6_M1382)"
FT VARIANT 110
FT /note="H -> N (in plasmid pINV_F6_M1382)"
FT VARIANT 136..137
FT /note="TK -> SE (in plasmid pINV_F6_M1382)"
FT VARIANT 144
FT /note="D -> N (in plasmid pINV_F6_M1382)"
FT VARIANT 152..154
FT /note="GPV -> EPI (in plasmid pINV_F6_M1382)"
FT VARIANT 155
FT /note="N -> D (in plasmid pCP301)"
FT VARIANT 159..161
FT /note="SHH -> NYN (in plasmid pINV_F6_M1382)"
FT VARIANT 166
FT /note="S -> G (in plasmid pCP301 and plasmid
FT pINV_F6_M1382)"
FT VARIANT 200..201
FT /note="RD -> SK (in plasmid pINV_F6_M1382)"
FT VARIANT 200
FT /note="R -> S (in plasmid pCP301)"
FT VARIANT 252
FT /note="V -> A (in plasmid pINV_F6_M1382)"
FT VARIANT 260
FT /note="P -> Q (in plasmid pINV_F6_M1382)"
FT VARIANT 300
FT /note="S -> K (in plasmid pINV_F6_M1382)"
FT VARIANT 300
FT /note="S -> N (in plasmid pCP301)"
FT VARIANT 304
FT /note="G -> E (in plasmid pINV_F6_M1382)"
FT VARIANT 311
FT /note="G -> E (in plasmid pCP301 and plasmid
FT pINV_F6_M1382)"
FT VARIANT 325
FT /note="K -> Q (in plasmid pINV_F6_M1382)"
FT VARIANT 328
FT /note="S -> K (in plasmid pINV_F6_M1382)"
FT VARIANT 359
FT /note="D -> G (in plasmid pINV_F6_M1382)"
FT VARIANT 405..407
FT /note="VNN -> LNK (in plasmid pINV_F6_M1382)"
FT VARIANT 406..407
FT /note="NN -> TK (in plasmid pCP301)"
FT VARIANT 424..425
FT /note="VT -> MA (in plasmid pINV_F6_M1382)"
FT VARIANT 424
FT /note="V -> M (in plasmid pCP301)"
FT VARIANT 519
FT /note="S -> A (in plasmid pINV_F6_M1382)"
FT MUTAGEN 439
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12356723"
SQ SEQUENCE 538 AA; 59833 MW; 304D27839C64CF96 CRC64;
MHITNLGLHQ VSFQSGDSYK GAEETGKHKG VSVISYQRVK NGERNKGIEA LNRLYLQNQT
SLTGKSLLFA RDKAEVFCEA IKLAGGDTSK IKAMMERLDT YKLGEVNKRH INELNKVISE
EIRAQLGIKN KKELQTKIKQ IFTDYLNNKN WGPVNKNISH HGKNYSFQLT PASHMKIGNK
NIFVKEYNGK GICCASTRER DHIANMWLSK VVDDEGKEIF SGIRHGVISA YGLKKNSSER
AVAARNKAEE LVSAALYSRP ELLSQALSGK TVDLKIVSTS LLTPTSLTGG EESMLKDQVS
ALKGLNSKRG GPTKLLIRNS DGLLKEVSVN LKVVTFNFGV NELALKMGLG WRNVDKLNDE
SICSLLGDNF LKNGVIGGWA AEAIEKNPPC KNDVIYLANQ IKEIVNNKLQ KNDNGEPYKL
SQRVTLLAYT IGAVPCWNCK SGKDRTGMQD AEIKREIIRK HETGQFSQLN SKLSSEEKRL
FSTILMNSGN MEIQEMNTGV PGNKVMKKLP LSSLELSYSE RIGDPKIWNM VKGYSSFV
