ID   Q3AYD1_SYNS9            Unreviewed;       700 AA.
AC   Q3AYD1;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN   OrderedLocusNames=Syncc9902_0930 {ECO:0000313|EMBL:ABB25896.1};
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB25896.1, ECO:0000313|Proteomes:UP000002712};
RN   [1] {ECO:0000313|Proteomes:UP000002712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000097; ABB25896.1; -; Genomic_DNA.
DR   RefSeq; WP_011359732.1; NC_007513.1.
DR   AlphaFoldDB; Q3AYD1; -.
DR   STRING; 316279.Syncc9902_0930; -.
DR   KEGG; sye:Syncc9902_0930; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_1_3; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000002712; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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; PTHR11804:SF83; LD37516P; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 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          43..158
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          238..696
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   700 AA;  77692 MW;  B0D471EAA1B39D41 CRC64;
     MAHTSSPLLQ GQGLPEFGAI TSDQVKQDIP VILRQVDEAF TAYESRLEAI LNSQTALDWA
     TVMGPLQEFG ERLRWSWGVV SHLNGVCNSS ELRTAHAEQQ PEVVRLGNRL GQSQVLHSAL
     TRLQESPVVA LTPTQSRILR SELLSMQHRG VGLCGDDKAK FNEASERLAA LSTQFGNHVL
     DATQQWTLKL TSREEVAGLP QRALEALASA AKEAGDSAAT AEAGPWLLGL DMPRYLPFLT
     HANNRSVRET AYRAHVGRAS SGEHDNRALI EEILSLRGQQ ATRLGYAHWA DVSLASKMAK
     DVDAVEGLLE ELRVAAFPAA ERELDDLKAL AQRHGAAEAE ELAPWDLPYW SEKLRQERFD
     LDQEALRPWF PLPQVLDGLF GLCNRLFDVV IEAADGEAPI WHEDVRYFRV QRQDGTPLAS
     FYLDPYSRPA SKRGGAWMDE CLGRRTNPDG SRVLPVAYLI CNQTPPVGDT PSLMSFEEVE
     TLFHEFGHGL QHMLTTVDEP EAAGISNVEW DAVELPSQFM ENWCLDRATL MGMARHWQTN
     EPLPEEEFQK LRRSRTFNAG LATLRQVHFA LSDLRLHSRW TPELGITPDA LRRDVATTTT
     VMEPIPEDQF LCAFGHIFAG GYSAGYYSYK WAEVLSADAF AAFEDAGLDD EQKVQSTGAL
     FRDTVLSLGG SRSPSEVFEA FRGRPASTDA LIRHSGLVNA
//