PPZA_ASPFC
ID PPZA_ASPFC Reviewed; 540 AA.
AC B0XUR7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Serine/threonine-protein phosphatase ppzA {ECO:0000303|PubMed:25943523};
DE EC=3.1.3.16 {ECO:0000305|PubMed:25943523};
GN Name=ppzA {ECO:0000303|PubMed:25943523}; ORFNames=AFUB_021020;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25943523; DOI=10.1534/g3.115.016766;
RA Winkelstroeter L.K., Dolan S.K., Fernanda Dos Reis T., Bom V.L.,
RA Alves de Castro P., Hagiwara D., Alowni R., Jones G.W., Doyle S.,
RA Brown N.A., Goldman G.H.;
RT "Systematic Global Analysis of Genes Encoding Protein Phosphatases in
RT Aspergillus fumigatus.";
RL G3 (Bethesda) 5:1525-1539(2015).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=28753224; DOI=10.1111/cmi.12770;
RA Manfiolli A.O., de Castro P.A., Dos Reis T.F., Dolan S., Doyle S.,
RA Jones G., Riano Pachon D.M., Ulas M., Noble L.M., Mattern D.J.,
RA Brakhage A.A., Valiante V., Silva-Rocha R., Bayram O., Goldman G.H.;
RT "Aspergillus fumigatus protein phosphatase PpzA is involved in iron
RT assimilation, secondary metabolite production, and virulence.";
RL Cell. Microbiol. 19:0-0(2017).
CC -!- FUNCTION: Catalytic subunit of protein phosphatase Z (PPZ) involved in
CC iron assimilation (PubMed:25943523, PubMed:28753224). Regulates
CC secondary metabolites production, including gliotoxin, pyripyropene A,
CC fumagillin, fumiquinazoline A, triacetyl-fusarinine C, and helvolic
CC acid (PubMed:25943523, PubMed:28753224). Plays a key role in
CC pathogenicity (PubMed:28753224). {ECO:0000269|PubMed:25943523,
CC ECO:0000269|PubMed:28753224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000305|PubMed:25943523};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000305|PubMed:25943523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000305|PubMed:25943523};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC Evidence={ECO:0000305|PubMed:25943523};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P36873};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P36873};
CC -!- SUBUNIT: Interacts with at least 54 proteins, of which 31 are detected
CC only after iron starvation and 22 are detected only in control
CC conditions (PubMed:28753224). Only the regulatory subunit of the
CC protein phosphatase PP1 (Afu1g04800/AFUB_005140) interacts with ppzA in
CC both conditions (PubMed:28753224). {ECO:0000269|PubMed:28753224}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Reduces sidC and sidG expression, slightly
CC increases gliotoxin production, decreases growth in iron starvation
CC conditions and leads to reduced conidiation at 44 degrees Celsius
CC (PubMed:25943523). Reduces the production of pyripyropene A,
CC fumagillin, fumiquinazoline A, triacetyl-fusarinine C, and helvolic
CC acid (PubMed:28753224). Abolishes virulence in a neutropenic murine
CC model of invasive pulmonary aspergillosis (PubMed:28753224).
CC {ECO:0000269|PubMed:25943523, ECO:0000269|PubMed:28753224}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC {ECO:0000305}.
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DR EMBL; DS499595; EDP54052.1; -; Genomic_DNA.
DR EnsemblFungi; EDP54052; EDP54052; AFUB_021020.
DR VEuPathDB; FungiDB:AFUB_021020; -.
DR HOGENOM; CLU_004962_3_1_1; -.
DR PhylomeDB; B0XUR7; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR011159; PPPtase_PPZ/Ppq1.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PIRSF; PIRSF000909; PPPtase_PPZ; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase.
FT CHAIN 1..540
FT /note="Serine/threonine-protein phosphatase ppzA"
FT /id="PRO_0000454887"
FT DOMAIN 258..540
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 300
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 239
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 267
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 267
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 423
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
SQ SEQUENCE 540 AA; 59548 MW; 140BF85438C54BC3 CRC64;
MGQSHSKGNS GPGDSLQSYP SFSRSDTKES LRSLRGSIRS KIRSSDSPRG STAGLSDDKS
DAASVKSTTS RRSSTNQSVQ SPDDTPSQPD APEPPPSPSL SSSLKRGHKD VNAMQQSGEV
DHVSDVPPTG AAPTGPSTQK VGESILIKRE NQLNPILDFI MNAPLETSGS PGMGMGALKS
IDLDDMISRL LDAGYSTKVT KTVCLKNAEI MAICSAAREL FLSQPALLEL SAPVKIVGDV
HGQYTDLIRL FEMCGFPPAS NYLFLGDYVD RGKQSLETIL LLLCYKLKYP ENFFLLRGNH
ECANVTRVYG FYDECKRRCN IKIWKTFIDT FNCLPIAATV AGKIFCVHGG LSPSLSHMDD
IRGIARPTDV PDYGLLNDLL WSDPADMEED WEPNERGVSY CFGKKVIMNF LQRHDFDLVC
RAHMVVEDGY EFYQDRILVT VFSAPNYCGE FDNWGAIMSV SGELLCSFEL LKPLDSTALK
NHIKKGRKER NSMLSSPVSP PLLRFVVAKE DHNLFVQHRR DACGLFLAYP SLVTSWGISR
