ID   A0A0C9PZA2_9BACT        Unreviewed;       594 AA.
AC   A0A0C9PZA2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=BROSI_A0382 {ECO:0000313|EMBL:GAN31878.1};
OS   Candidatus Brocadia sinica JPN1.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Brocadia.
OX   NCBI_TaxID=1197129 {ECO:0000313|EMBL:GAN31878.1, ECO:0000313|Proteomes:UP000032309};
RN   [1] {ECO:0000313|EMBL:GAN31878.1, ECO:0000313|Proteomes:UP000032309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPN1 {ECO:0000313|EMBL:GAN31878.1,
RC   ECO:0000313|Proteomes:UP000032309};
RA   Oshiki M., Shinyako-Hata K., Satoh H., Okabe S.;
RT   "Draft Genome Sequence of an Anaerobic Ammonium-Oxidizing Bacterium,
RT   "Candidatus Brocadia sinica".";
RL   Genome Announc. 3:e00267-15(2015).
CC   -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC       bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU368091};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC   -!- SIMILARITY: Belongs to the peptidase M3B family.
CC       {ECO:0000256|RuleBase:RU368091}.
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:GAN31878.1}.
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; BAFN01000001; GAN31878.1; -; Genomic_DNA.
DR   RefSeq; WP_052561839.1; NZ_BAFN01000001.1.
DR   AlphaFoldDB; A0A0C9PZA2; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000032309; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09608; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR004438; Peptidase_M3B.
DR   NCBIfam; TIGR00181; pepF; 1.
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; PF08439; Peptidase_M3_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368091};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368091};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU368091};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032309};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          113..182
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          202..577
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   594 AA;  69064 MW;  A911F9899BA6781A CRC64;
     MNKNKTRDQI EGKYKWDLSV LYASDDTWEE DYRKVEKGLP QLLEFKGSLA DPRKLGQFMQ
     FYINHSIVRE NLYVYAYVRF FEDTRNAVYE EMKGRIELLA SKISAQTVFI KKELSSLSQD
     DIDTMISENS HLAGYRFFLE SYARYNPHIL SEETETVLAE LEIALKKPDD IFSAYNNNNI
     SFGEFEHKEE IIRLSHARYV QLLESPDRAL RQKAFDYYYR PYLQNIDVLA NTYAANVLAN
     IKMAKVRNYS SMLEMSLFPD YVPTTVFTNL IEVAKENIDV ISEFNALKQE ELGIEELHFY
     DNYVPLVREV DKKYSYEEAI ELVRTALEPL GAEYLKKYDS TVCAGVIDVF ESPGKRSGAF
     SWGSYASRGL IFLNYTEKFS DVSTFAHEFG HCLHRDYSIE NQPYIYYQNP IFLAEIASAF
     NEALLFDHMS KIAESREEKK FFLYHSMKRI EATFYRQTMF ANFERDIHEM AESGKVLMAK
     SITGVYRKNL EAYLGKGMVI DEQLNYEWAR IPHFYNAFYV YKYATSLSAA IALSQRVTSG
     EEGAVEDYLT FLGRGSHKEP LEILKDAGID LSGKEPYAVT VDKFRKLLKE YKAL
//