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Database: UniProt
Entry: A0A0B0EIV5_9BACT
LinkDB: A0A0B0EIV5_9BACT
Original site: A0A0B0EIV5_9BACT 
ID   A0A0B0EIV5_9BACT        Unreviewed;       594 AA.
AC   A0A0B0EIV5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=SCABRO_03211 {ECO:0000313|EMBL:KHE91053.1};
OS   Candidatus Scalindua brodae.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Scalinduaceae; Scalindua.
OX   NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE91053.1, ECO:0000313|Proteomes:UP000030652};
RN   [1] {ECO:0000313|EMBL:KHE91053.1, ECO:0000313|Proteomes:UP000030652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU1 {ECO:0000313|EMBL:KHE91053.1};
RA   Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT   "Draft genome of anammox bacterium scalindua brodae, obtained using
RT   differential coverage binning of sequence data from two enrichment
RT   reactors.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KHE91053.1}.
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DR   EMBL; JRYO01000221; KHE91053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B0EIV5; -.
DR   PATRIC; fig|237368.3.peg.3472; -.
DR   eggNOG; COG1164; Bacteria.
DR   Proteomes; UP000030652; 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   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          203..577
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   594 AA;  68997 MW;  2B3A70AB95043C2B CRC64;
     MNKNKTRDEI EDKYKWDLSV LYTSDDFWEE DYRKVEKELS QLLEFKGTLA DFSKLEQFMR
     TYIDFSIVKE NLYVYANVRF FEDTRNAIYE EMKGRIELLV SRISAETVFI KKELSSLSEK
     EIDKLIHENS RLSEYRFFLD GYARYNPHIL SEESETVLAE LGIALGKPDD IFSAFNDNNI
     SFDVFKHKGE EIHLSHAKYA QILESPDREL RQKAFEYYYK PFLQNIDVLA NTYATTVLTN
     IKLTKIRNYK SMLESALFPD YLPTTVFTNL VDVVKENIDV VSDFNALKQE ALGVEELHFY
     DNYIPLVADV DKAYSYEETI DLVRTALEPL GPEYSRRYDA TVNARVIDVF ESVGKRSGAF
     SWGSYASRGL VFLNHTGKFS DVSTFAHEFG HCLHRDYSIE NQPYIYYQNP IFLAEIASTF
     NEALLFDHMS KIAVSREEKK FFLYHNMKRI EATFFRQTMF ASFEKEVHEM AESGKVLIAK
     SITDVYRKNL EAYLGNGMVI DEQLHCEWAR IPHFYNAFYV YKYATSLSAA IALAERVSSG
     EARAVDDYLS FLGAGSHKEP LAILKDAGVD MTGKEVYEVT VNKFRKLMEE YKSL
//
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