ID   S6HWY7_9GAMM            Unreviewed;       616 AA.
AC   S6HWY7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:EPJ49856.1};
GN   ORFNames=OFPI_22270 {ECO:0000313|EMBL:EPJ49856.1};
OS   Osedax symbiont Rs2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ49856.1, ECO:0000313|Proteomes:UP000014830};
RN   [1] {ECO:0000313|EMBL:EPJ49856.1, 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   -!- 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|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:EPJ49856.1}.
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DR   EMBL; ASZI01000170; EPJ49856.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6HWY7; -.
DR   PATRIC; fig|1330035.3.peg.2131; -.
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   Gene3D; 1.10.1370.30; -; 2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR   Pfam; PF01432; Peptidase_M3; 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          151..547
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   616 AA;  69535 MW;  AEBF9046300DCB18 CRC64;
     MNPTEYFNQL NQDYIAVHGP KEELFWTTYM GVSDDHSGCA AAETRWNEFI ANGQRIPELR
     QQLAKLNQSQ EPTLSGELQQ VKKGLEGWLA MYQSNAIESQ SAQQQKAELI KAEAQLFEKR
     QNYAMHYTDA QGVQVEASMG VLRANIYSDN NEAVRQSSHQ ALLDLEDWVL DNGYIELVRQ
     RNQFARSLGF SNFFDYSIEK TEQMSTEQLF NILDDFELRT RDRNVRSIAE LAAQHGEQSL
     QGHNFNYTWG GDSMRELDPY VPFKNSLRQW VESFGRLNID YSSAELTLDL LDRKGKYQNG
     FCHGPMPSYF DNGDWVAGKI NFTSNAKPDQ VGSGYDGLNT LFHEGGHAAH FANVTLNSPC
     FSHEFPPTSM AYAETQSMFC DSLLEDADWL KLYAKDAQGN SVPDSVIKSL IESKQPFRAF
     GERNILLVPY FEQALYATPD NLLSAPLIKK LARDLEYKIT GLAISPRPLL AIPHLLSNDS
     ACSYQGYLLA NMAVFQTRAY FTQRFGYLTD NPEIGPLLAK HYWNAGNSVD HAAGVKSLTG
     EGFNPKYLAD VCNLSVTAAW EEDRARIVAL KGRPRTVVEP LNANITIVDG KKVLANNSES
     NRVMCEQFEN YIQANY
//