ID   A0A0U1NKY2_9RHOB        Unreviewed;       456 AA.
AC   A0A0U1NKY2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Protease 3 {ECO:0000313|EMBL:CRK75348.1};
DE            EC=3.4.24.55 {ECO:0000313|EMBL:CRK75348.1};
GN   Name=ptrA_1 {ECO:0000313|EMBL:CRK75348.1};
GN   ORFNames=NIG5292_01392 {ECO:0000313|EMBL:CRK75348.1};
OS   Nereida ignava.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Nereida.
OX   NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK75348.1, ECO:0000313|Proteomes:UP000048949};
RN   [1] {ECO:0000313|EMBL:CRK75348.1, ECO:0000313|Proteomes:UP000048949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK75348.1,
RC   ECO:0000313|Proteomes:UP000048949};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CVQV01000005; CRK75348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1NKY2; -.
DR   STRING; 282199.GCA_001049735_01391; -.
DR   Proteomes; UP000048949; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CRK75348.1};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CRK75348.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000048949};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..456
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006712233"
FT   DOMAIN          39..184
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          195..377
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   456 AA;  50059 MW;  13F1AFC11F3CF52C CRC64;
     MRLASLMLAS LLWMPLTAAT TAAAADNVTT FALDNGMEVV VIEDHRAPVV VHMVWYRAGA
     ADEDPGKSGI AHFLEHLLFK ATDDMEAGVF SKVVAANGGR DNAFTSYDYT AYFQRVAADR
     LELMMRMESD RMRDLRLTED DIETERNVVL EERNQRTEND PGSLFGEQRM AAQYQNHPYG
     IPVIGWKHEV AQLGLDDALA YYQRFYAPNN AVLVVAGDVY PDEVKRLAET YYGVLEPTKD
     LTARARPTEP PHRAERRLVF EDPRVAQPYV IRTYLAPERD SGAQEKAAAL TLLSELLGGN
     PATSFLGQQL QFDSQDAVYT GAFYSGLSLD DTTFGVVMVP TPGISLSEAE AKLDAAIAQF
     LEAGIDEEQL ARIKAQLRAS EIYGRDSVQS LARTYGAGLT SGLTVADIQA WPDVLAAVTS
     DDILQAAWAL FSDRKVAVTG YLRSPTSPEA ASQVSQ
//