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Database: UniProt
Entry: A0A0J6NIX2_9NEIS
LinkDB: A0A0J6NIX2_9NEIS
Original site: A0A0J6NIX2_9NEIS 
ID   A0A0J6NIX2_9NEIS        Unreviewed;       774 AA.
AC   A0A0J6NIX2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Dictomallein {ECO:0000256|ARBA:ARBA00018800};
GN   ORFNames=VK98_14185 {ECO:0000313|EMBL:KMN81308.1};
OS   Chromobacterium sp. LK11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN81308.1, ECO:0000313|Proteomes:UP000036114};
RN   [1] {ECO:0000313|EMBL:KMN81308.1, ECO:0000313|Proteomes:UP000036114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LK11 {ECO:0000313|EMBL:KMN81308.1,
RC   ECO:0000313|Proteomes:UP000036114};
RA   Chan X.Y.;
RT   "Draft genome of Chromobacterium aquaticum LK11.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01031};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01031};
CC   -!- SIMILARITY: Belongs to the dictomallein family.
CC       {ECO:0000256|ARBA:ARBA00005693}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMN81308.1}.
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DR   EMBL; LDUR01000022; KMN81308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6NIX2; -.
DR   STRING; 1628212.VK98_14185; -.
DR   PATRIC; fig|1628212.3.peg.1933; -.
DR   Proteomes; UP000036114; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.1230; -; 2.
DR   InterPro; IPR019503; Peptidase_M66_dom.
DR   InterPro; IPR048990; StcE_b-sandwich.
DR   InterPro; IPR022218; TagA_dom.
DR   PANTHER; PTHR39540; -; 1.
DR   PANTHER; PTHR39540:SF1; DICTOMALLEIN-1-RELATED; 1.
DR   Pfam; PF10462; Peptidase_M66; 1.
DR   Pfam; PF20944; StcE_b-sandwich; 1.
DR   Pfam; PF12561; TagA; 1.
DR   PROSITE; PS51694; PEPTIDASE_M66; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01031};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01031};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW   ProRule:PRU01031};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01031}; Reference proteome {ECO:0000313|Proteomes:UP000036114};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01031}.
FT   DOMAIN          271..527
FT                   /note="Peptidase M66"
FT                   /evidence="ECO:0000259|PROSITE:PS51694"
FT   ACT_SITE        421
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT   BINDING         420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT   BINDING         424
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT   BINDING         430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
SQ   SEQUENCE   774 AA;  82646 MW;  41B431DAFC6D9267 CRC64;
     MAGQAAGYAA VANAWPFNAV TPRNDLSGAF EAEVSFAQSQ VMPAGAGIAG DSQPHLVAGR
     QALLMLRPIS AISANKPLQV AVKDKSGATL GTLSLNPPDK QPKTAYFVDG APEGGIDFTP
     PSGAQTTISS NADLAKLDDP NGAFLRGKLA ANVMVNIQTA DGSWVKTVYL PADPAFEGKM
     IRFQSQAGYG STVRYSSRSV DVSRGDTLLF KYVNGQWFRQ GELDNNRIVY SQDLWSAVLP
     AAWIKPGMSL QFSHESRSGA LSKLEVGPAT QLQINTIDIG MLVEPRGAFA FANDPDAHRE
     YLQTAPLNQL LVAQYAPVHL KEVMLPDGTR LTQQDPSQGG WHTGTMREDI GKELISTGIN
     YANYGVNSTA GRGAAFPLVA ALLTAHNSQG RYANGVQVHG GSGGGGVVTL DESLGNEFSH
     EVGHNYGLGH YVGGFDGSVH RPAGAINSSW GWDADLKRFL PNFSGVVSNQ NTCMPEGKPC
     QSPFAGRSYG LDAMAGGSPM SAVNRFTLYT PYAAKQIQRF LESKPVFDSA SATGFSQWNA
     STQSMDTYRH LISPDTTTVP LEKLSEAYLA EVLGQADRAL IKMEDGYWIR EVKAPAASAA
     NKGKFITINS RATYATSLQA PGQTFPVAGQ SGDNHFVSDG RQWLKTQSIE TERKPQRFGV
     PVTTLLGYYD PEMKLPSYVY PALRGAYGYS YPDDGASASP AQCQLQVDTA SGQLKYKLQS
     ARVNGEVMNK FHVNVPSALQ PQNVKVVCGG KSLASKTVPA ASGALRYTVN GVLQ
//
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