APRA_PSEE4
ID APRA_PSEE4 Reviewed; 485 AA.
AC Q1ID47;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Metalloprotease AprA {ECO:0000303|PubMed:16789834};
DE EC=3.4.24.- {ECO:0000269|PubMed:16789834};
GN Name=aprA {ECO:0000303|PubMed:16789834, ECO:0000312|EMBL:CAK14412.1};
GN OrderedLocusNames=PSEEN1550 {ECO:0000312|EMBL:CAK14412.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16789834; DOI=10.1371/journal.ppat.0020056;
RA Liehl P., Blight M., Vodovar N., Boccard F., Lemaitre B.;
RT "Prevalence of local immune response against oral infection in a
RT Drosophila/Pseudomonas infection model.";
RL PLoS Pathog. 2:E56-E56(2006).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21980286; DOI=10.1371/journal.ppat.1002259;
RA Opota O., Vallet-Gely I., Vincentelli R., Kellenberger C., Iacovache I.,
RA Gonzalez M.R., Roussel A., van der Goot F.G., Lemaitre B.;
RT "Monalysin, a novel beta-pore-forming toxin from the Drosophila pathogen
RT Pseudomonas entomophila, contributes to host intestinal damage and
RT lethality.";
RL PLoS Pathog. 7:E1002259-E1002259(2011).
CC -!- FUNCTION: Secreted protease which is important for P.entomophila to
CC counteract the local immune response of Drosophila (PubMed:16789834).
CC Can degrade antimicrobial peptides (AMPs), e.g. Diptericin and Cecropin
CC A. Thus, protects P.entomophila from the Drosophila antimicrobial
CC peptides produced by the gut innate immune response, and promotes
CC bacterial persistence in the Drosophila gut and killing of the host
CC (PubMed:16789834). Is responsible for maturation of pro-Monalysin to
CC the active toxin Monalysin, by cleaving its N-terminus
CC (PubMed:21980286). {ECO:0000269|PubMed:16789834,
CC ECO:0000269|PubMed:21980286}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q03023};
CC Note=Binds 8 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:Q03023};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q03023};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q03023};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16789834,
CC ECO:0000269|PubMed:21980286}. Note=Is probably secreted via the
CC associated Type 1 transporter encoded by aprDEF.
CC {ECO:0000305|PubMed:16789834}.
CC -!- INDUCTION: Is regulated by the GacS/GacA two-component system that
CC controls P.entomophila pathogenicity. Seems also regulated by PrtR.
CC {ECO:0000269|PubMed:16789834}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of aprA attenuates both the capacity
CC to persist in the host and pathogenicity. The deletion mutants are able
CC to survive to wild-type levels in immune-deficient Relish flies,
CC indicating that the protease plays an important role in protection
CC against the Drosophila Imd-dependent immune response. Moreover, they
CC persist less well than wild-type bacteria in imd flies over-expressing
CC Diptericin (PubMed:16789834). Pro-Monalysin is found in supernatant
CC derived from the aprA-deletion mutant while the mature form
CC predominates in supernatant from wild-type P.entomophila
CC (PubMed:21980286). {ECO:0000269|PubMed:16789834,
CC ECO:0000269|PubMed:21980286}.
CC -!- SIMILARITY: Belongs to the peptidase M10B family. {ECO:0000305}.
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DR EMBL; CT573326; CAK14412.1; -; Genomic_DNA.
DR RefSeq; WP_011532827.1; NC_008027.1.
DR AlphaFoldDB; Q1ID47; -.
DR SMR; Q1ID47; -.
DR STRING; 384676.PSEEN1550; -.
DR MEROPS; M10.062; -.
DR EnsemblBacteria; CAK14412; CAK14412; PSEEN1550.
DR KEGG; pen:PSEEN1550; -.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_025059_1_1_6; -.
DR OMA; WYLINSS; -.
DR OrthoDB; 1907192at2; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IMP:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031638; P:zymogen activation; IMP:UniProtKB.
DR CDD; cd04277; ZnMc_serralysin_like; 1.
DR Gene3D; 2.150.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR016294; Pept_M10B.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR034033; Serralysin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF00353; HemolysinCabind; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR PIRSF; PIRSF001205; Peptidase_M10B; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; SSF51120; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Metal-binding; Metalloprotease; Protease; Repeat;
KW Secreted; Toxin; Virulence; Zinc.
FT CHAIN 1..485
FT /note="Metalloprotease AprA"
FT /id="PRO_0000439891"
FT REPEAT 347..364
FT /note="Hemolysin-type calcium-binding 1"
FT /evidence="ECO:0000250|UniProtKB:A0A0C5CJR8"
FT REPEAT 365..382
FT /note="Hemolysin-type calcium-binding 2"
FT /evidence="ECO:0000250|UniProtKB:A0A0C5CJR8"
FT REPEAT 383..395
FT /note="Hemolysin-type calcium-binding 3"
FT /evidence="ECO:0000250|UniProtKB:A0A0C5CJR8"
FT ACT_SITE 188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 367
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:Q03023"
SQ SEQUENCE 485 AA; 50931 MW; D3A3513DFB87C733 CRC64;
MSKVKESAIV SATSALQPQG PSSSYGLINS FAHQYDRGGA NVNGKPSYTV DQAANYLLRD
GAAWKDLNKD GTISLSYTFL TKAPSDFYSR GLGTFSQFSD LQKGQAKLAM QSWADVAKVT
FTEAASGGDG HMTFGNFSAS NGGAAFAYLP FDMPGSHKGE SWYLINSSYQ VNTTPGTGNY
GRQTLTHEIG HVLGLSHPGD YNAGEGNPTY RDATYAQDTR GYSVMSYWSE SNTGQNFVKA
GGQYYASAPL MDDIAAIQKL YGANYATRSG DTVYGFNSNA DRDFYSATSS SSKLVFSVWD
GGGNDTFDFS GFTQNQKINL NETSFSDVGG MIGNVSIAKG VTIENAFGGS GNDLLIGNAL
ANVLKGGAGN DIIYGGGGAD QLWGGTGADT FVFGAISDST KAAPDRIMDF TSGQDKIDLS
AISAFAVNKL PLQFVNAFTG HAGEAVLSYD QGTNLGSLSI DFTGNSSADF LVTTVGQAAV
TDIVV
