SITA_ASPFU
ID SITA_ASPFU Reviewed; 388 AA.
AC Q4WM22;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Serine/threonine-protein phosphatase sitA {ECO:0000303|PubMed:25911225};
DE EC=3.1.3.16 {ECO:0000255|RuleBase:RU004273};
GN Name=sitA {ECO:0000303|PubMed:25911225}; ORFNames=AFUA_6G11470;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25911225; DOI=10.1128/ec.00008-15;
RA Bom V.L., de Castro P.A., Winkelstroeter L.K., Marine M., Hori J.I.,
RA Ramalho L.N., dos Reis T.F., Goldman M.H., Brown N.A., Rajendran R.,
RA Ramage G., Walker L.A., Munro C.A., Rocha M.C., Malavazi I., Hagiwara D.,
RA Goldman G.H.;
RT "The Aspergillus fumigatus sitA phosphatase homologue is important for
RT adhesion, cell wall integrity, biofilm formation, and virulence.";
RL Eukaryot. Cell 14:728-744(2015).
CC -!- FUNCTION: Protein phosphatase that acts as a modulator of pkcA/mpkA
CC activity involved in the cell wall integrity pathway (PubMed:25911225).
CC Plays an important role in regulation of adhesion, cell wall integrity,
CC biofilm formation, and virulence (PubMed:25911225).
CC {ECO:0000269|PubMed:25911225}.
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:0000255|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P67775};
CC -!- DISRUPTION PHENOTYPE: Leads to decreased mpkA phosphorylation levels,
CC increased sensitivity to cell wall-damaging agents, increased levels of
CC beta-(1,3)-glucan and chitin, impaired in biofilm formation, and
CC decreased protein kinase C activity (PubMed:25911225). Increases also
CC sensitivity to several metals and ions, such as MnCl(2), CaCl(2), and
CC LiCl, but it is more resistant to ZnSO(4) (PubMed:25911225). Impeairs
CC the virulencein a murine model of invasive pulmonary aspergillosis and
CC induces an augmented tumor necrosis factor alpha response in mouse
CC macrophages (PubMed:25911225). {ECO:0000269|PubMed:25911225}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V)
CC subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL88992.2; -; Genomic_DNA.
DR RefSeq; XP_751030.2; XM_745937.2.
DR SMR; Q4WM22; -.
DR STRING; 746128.CADAFUBP00007552; -.
DR EnsemblFungi; EAL88992; EAL88992; AFUA_6G11470.
DR GeneID; 3508335; -.
DR KEGG; afm:AFUA_6G11470; -.
DR VEuPathDB; FungiDB:Afu6g11470; -.
DR eggNOG; KOG0373; Eukaryota.
DR HOGENOM; CLU_004962_8_3_1; -.
DR InParanoid; Q4WM22; -.
DR OMA; CQNKYGN; -.
DR OrthoDB; 808922at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0043708; P:cell adhesion involved in biofilm formation; IMP:AspGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:EnsemblFungi.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:AspGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:EnsemblFungi.
DR GO; GO:2001211; P:negative regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:EnsemblFungi.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:EnsemblFungi.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IEA:EnsemblFungi.
DR GO; GO:1903379; P:regulation of mitotic chromosome condensation; IEA:EnsemblFungi.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:EnsemblFungi.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Metal-binding; Reference proteome; Virulence.
FT CHAIN 1..388
FT /note="Serine/threonine-protein phosphatase sitA"
FT /id="PRO_0000453182"
FT REGION 86..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 67
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 69
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
SQ SEQUENCE 388 AA; 43535 MW; 931FB3CFA3E16037 CRC64;
MVDNKIPEPG PAKLKRNAGP DEWLEAAKDC KYLSEQHMKQ LCEIVKEYMM EESNIQPVST
PVTICGDIHG QFYDLLELFR VSGGMPDGSE AEAPKTQSAV ITSDDIEPPS TISDPKLRKK
LRNTFAPEDG SEDSSASQRD RSSSSGSRDV ELKRNFVFLG DYVDRGYFSL ETLTLLLCLK
AKYPDRVTLV RGNHESRQIT QVYGFYEECF QKYGNASVWK ACCQVFDFMT LGAIIDGRVL
CVHGGLSPEI RTLDQVRVVA RAQEIPHEGA FCDLVWSDPD DVETWAVSPR GAGWLFGDKV
ADEFCHVNDL TLIARAHQLV NEGYKYHFAN QNVVTVWSAP NYCYRCGNLA SVCEIGDDLK
PTFKLFSAVS DDQRHVPVSR PGRSEYFL
