ASPN_XANCP
ID ASPN_XANCP Reviewed; 417 AA.
AC Q8PC00;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Peptidyl-Asp metalloendopeptidase {ECO:0000312|EMBL:AAM40265.1};
DE EC=3.4.24.33;
DE AltName: Full=Endopeptidase Asp-N {ECO:0000250|UniProtKB:Q9R4J4};
DE Flags: Precursor;
GN OrderedLocusNames=XCC0955;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1] {ECO:0000312|EMBL:AAM40265.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- FUNCTION: Metalloprotease, specifically cleaves on the N-terminal side
CC of aspartyl, glutamyl and cysteic acid residues.
CC {ECO:0000250|UniProtKB:Q9R4J4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid
CC bonds.; EC=3.4.24.33; Evidence={ECO:0000250|UniProtKB:Q9R4J4};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O75173};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75173};
CC -!- SIMILARITY: Belongs to the peptidase M72 family. {ECO:0000305}.
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DR EMBL; AE008922; AAM40265.1; -; Genomic_DNA.
DR RefSeq; NP_636341.1; NC_003902.1.
DR RefSeq; WP_011036169.1; NC_003902.1.
DR AlphaFoldDB; Q8PC00; -.
DR SMR; Q8PC00; -.
DR STRING; 340.xcc-b100_3396; -.
DR EnsemblBacteria; AAM40265; AAM40265; XCC0955.
DR KEGG; xcc:XCC0955; -.
DR PATRIC; fig|190485.4.peg.1029; -.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_658751_0_0_6; -.
DR OMA; CMVARAD; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..417
FT /note="Peptidyl-Asp metalloendopeptidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395561"
FT ACT_SITE 332
FT /evidence="ECO:0000250|UniProtKB:O75173,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75173,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75173,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75173,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 417 AA; 44137 MW; 09D2F53A8DE71F26 CRC64;
MKSKSMCTTV GLIAMCLAGS AAAAGKPLYQ TGPALSRSAA ATATAEPSLQ RVLSSPSTAN
AQVVQIDAGA VAPAEKLLEL QLDGQTITAT QAKVDALEGG DSIWYGNLGP RAGTRARTLS
GVDPLNSAIL VRSGDTVTGT IRYAGKLYRL RPLADGRHVL VQVDEQRMPQ EHPAEYSLLP
KFDMPNDGRV TAAQASSGSP ATIRVLVVAT NQAVTAYGGN MQSLVQLAVA EANQGYVNSN
VGITLQLARY ETTSYAETGN FTTDLQRFRV TNDGYMDSIH TSRNTYTADV GVIVLNNSSY
CGLASGIGST AATAFASVYW DCATGYYSFA HEIGHLQSAR HDAATDPSTS PFAYGHGYRY
GNSWRTIMAY ACPSGCPRLN YWSNPNISYN GVPMGNASTA DNQRVLVNTK ANIAAFR
