ID   S4Y7D4_SORCE            Unreviewed;       684 AA.
AC   S4Y7D4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN   ORFNames=SCE1572_40965 {ECO:0000313|EMBL:AGP40321.1};
OS   Sorangium cellulosum So0157-2.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP40321.1, ECO:0000313|Proteomes:UP000014803};
RN   [1] {ECO:0000313|EMBL:AGP40321.1, ECO:0000313|Proteomes:UP000014803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So0157-2 {ECO:0000313|EMBL:AGP40321.1,
RC   ECO:0000313|Proteomes:UP000014803};
RX   PubMed=23812535; DOI=10.1038/srep02101;
RA   Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA   Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT   "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT   milieu.";
RL   Sci. Rep. 3:2101-2101(2013).
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}.
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DR   EMBL; CP003969; AGP40321.1; -; Genomic_DNA.
DR   RefSeq; WP_020740060.1; NC_021658.1.
DR   AlphaFoldDB; S4Y7D4; -.
DR   STRING; 1254432.SCE1572_40965; -.
DR   KEGG; scu:SCE1572_40965; -.
DR   PATRIC; fig|1254432.3.peg.9255; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_1_7; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000014803; Chromosome.
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; 1.10.1370.40; -; 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          31..149
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          227..682
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   684 AA;  76527 MW;  A2E227EF5AF933FE CRC64;
     MTEATDNPLL SLGFEIPFDR IRSEHVEPAV RALLADARAR LEALIAAPGP RTYESTLAAL
     EAVTERLDRA MNVVSHLEST STTPELRAAY NAVQPEVSEF LSGIALNEGV YGALKAFAAT
     PEAAALTGPR RRFFKKTLDD FRRSGAELDP PGKKRLSEID VELATLTLRF SQNVLDATNA
     FEFVVEDPAR LAGLPPSAIE AARQSAQDKG VKGYRFTLQA PSYIPVLTHL DDASIRERFY
     RAYNTRATEG DHDNRPLIRR ILELRREKAK LLGYATFADL VLEDRMAKTG AEARRFVATL
     RERTEPVFAR EKDELAAFRR EIEGPGAPPI APWDVSYYAE KLRRARYDFD DEALRPYFPL
     DRVVSGLFEI AHRLYGVRIA PWQDAPTWHP TVRAYRLLEA DGAQSAAFYL DFAPREQKRD
     GAWMHGLVTG APSDGGRAAG EDARHLEVLA GSFTPPVGGR PALLNHREVE TLFHEFGHMM
     HHASSRVPIR SLAGTNVAWD FVELPSQIME NWCWEREALD LFARHHETGA PVPDDLLQRM
     RAARTFRAGA VTMRQLGFAE IDLALHVDWT PEHGDVVDFA REVLERYSPV PLPEGYAMIA
     GFSHLFSSPV GYAAGYYSYK WAEVLDADAF SRFQEEGLFS RKVGDAFRSQ VLALGDTQDP
     MDLYKSFRGR EPTLDALLQR SGLA
//