ID   S6HIE3_9GAMM            Unreviewed;       674 AA.
AC   S6HIE3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN   ORFNames=OFPI_28880 {ECO:0000313|EMBL:EPJ48603.1};
OS   Osedax symbiont Rs2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ48603.1, ECO:0000313|Proteomes:UP000014830};
RN   [1] {ECO:0000313|EMBL:EPJ48603.1, ECO:0000313|Proteomes:UP000014830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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}.
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:EPJ48603.1}.
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DR   EMBL; ASZI01000221; EPJ48603.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6HIE3; -.
DR   MEROPS; M03.004; -.
DR   PATRIC; fig|1330035.3.peg.2774; -.
DR   Proteomes; UP000014830; 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; 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:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000014830};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          34..144
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          218..672
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   674 AA;  76227 MW;  FFEBFDF987577693 CRC64;
     MSYSDISNAD LPNFSSLDSA AINSQLEQIL EYNNLQINQL LADNSCYNWD NLVAPLEQLN
     DTLANFWSPI SHLNAVCNTD ELRVAYNQAL PKLSAYYTAL GQNHQLYQAY AQIQRTELNS
     AQQKVLDNAL RDFKLSGVAL GEQQQQRFAQ IKLRTSELGT KFSENVLDAT QAWQKNITDL
     QQLAGMPELA LAAAKQAAQA KELPGYLLTL EFPSYLPVMT YCDNRALRQE MYTAFATRAS
     SASDSSGQQQ WDNSPIIDEL LALRKELATI LGFDSYAHYS LATKMANSPD DVLGFLNDLA
     QHSVSRARTE FATLRQFASA HSDQQLQAWD VGYYSEKLKQ QQFSISQEQL RPYFPMHKVL
     QGLFSITSRL FKFQITEIEQ FDSWHSDVKL FQISRDNTVI ARFYLDPYAR ANKRGGAWMD
     VCRTRRIDSQ GKLQLPTAYL VCNFNAPVGN DPALLTHSEL TTLFHEFGHG LHHMMTEMQY
     ADISGINGVP WDAVELPSQF LENWCWQPQA LAIISSHFSS GDTLPAELLD KLLEARNFQS
     AMAMVRQLEF SLFDYRLHLE YQPGESRVQP LLDEIRQQVA AVIPPAFNSF QNSFSHIFAG
     GYAAGYYSYK WAEVLSADAF SLFESKGIFH VETGQLFLNS ILQKGGSEEP LKLFVDFRGR
     EPDTEALLRH SGIL
//