ID   A0A0S8BJ80_9PROT        Unreviewed;       683 AA.
AC   A0A0S8BJ80;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   03-MAY-2023, entry version 25.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN   ORFNames=AMJ68_04755 {ECO:0000313|EMBL:KPK11694.1};
OS   Acidithiobacillales bacterium SG8_45.
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX   NCBI_TaxID=1703383 {ECO:0000313|EMBL:KPK11694.1, ECO:0000313|Proteomes:UP000053136};
RN   [1] {ECO:0000313|EMBL:KPK11694.1, ECO:0000313|Proteomes:UP000053136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_45 {ECO:0000313|EMBL:KPK11694.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of oligopeptides, with broad specificity. Gly or
CC         Ala commonly occur as P1 or P1' residues, but more distant residues
CC         are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-
CC         Pro-Ala is cleaved, but not Z-(Gly)(5).; EC=3.4.24.70;
CC         Evidence={ECO:0000256|ARBA:ARBA00024603};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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:KPK11694.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LJTU01000017; KPK11694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8BJ80; -.
DR   PATRIC; fig|1703383.3.peg.26; -.
DR   Proteomes; UP000053136; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045666; OpdA_N.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF19310; TOP_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          46..153
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          226..680
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   683 AA;  77332 MW;  63FA12D68FBF5174 CRC64;
     MTTSDTNPLL DFSGLPRFSQ IRPEHVAPAL EALLAEARAG RERLLSGNST PTWATLVQPL
     EDMNERIQRM WSPAGHLNAV MNSEALRKEY DACLPRLSAY STEVAQDERL YAAYKKIAAS
     DEYQAFDSAQ KKIIDNTLRD FRLAGAELNG DDKKRFAEIQ QKLAQLGSSF QNNVLDATQA
     WHLHLTEDNQ LAGLPEFARD MGAQAAKEKE LDGWCFTLDG PSYLAFMTYA DDRDLRQQLY
     QAYVCRASDQ GPNAGKWDNG PVIDEMLALR QEAAHLLGFD NYAEYSLATK MARDVSQVLG
     FLQDLAGRSR PTASQEFTEL SAFARDHDGT GTLSAWDIAY YSEKLREQRY AFSREELRPY
     FPESQVLPGM FEVIHRLYGM TVEPLTDVEI WHPDVKVYEI RQSDGIVRGR FYLDLYARSG
     KRGGAWMDDC VSRKRERDTV QTPTAYLVCN FSAPVGNKPA LFNHDEVITL FHEFGHGLHH
     MLTQVDYVSV SGINGVAWDA VELPSQFMEN WCWQREALDV IARHYETGKP IPDDLLDKMH
     AAKNFQSAMQ MVRQLEFALF DMRLHSEHDP QGDRSVQQLL DEVRAEVAVV PTPAFSRFQN
     GFGHIFAGGY AAGYYSYKWA EVLSADAFSK FEEQGIFNRK TGTEFLHSVL EQGGSRDPLE
     LFIEFRGREP DVEALLRHSG LAA
//