ID   R9C092_9BACI            Unreviewed;       596 AA.
AC   R9C092;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=A499_16121 {ECO:0000313|EMBL:EOR22769.1};
OS   Niallia nealsonii AAU1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1202533 {ECO:0000313|EMBL:EOR22769.1, ECO:0000313|Proteomes:UP000014030};
RN   [1] {ECO:0000313|EMBL:EOR22769.1, ECO:0000313|Proteomes:UP000014030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAU1 {ECO:0000313|EMBL:EOR22769.1,
RC   ECO:0000313|Proteomes:UP000014030};
RA   Joshi C.G., Duggirala S.M., Nathani N.M., Bhatt V.D., KaPatel J.A.,
RA   Parnerkar S.P.;
RT   "Whole genome shotgun sequencing of Bacillus nealsonii AAU1.";
RL   Submitted (MAR-2013) 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:EOR22769.1}.
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DR   EMBL; ASRU01000198; EOR22769.1; -; Genomic_DNA.
DR   RefSeq; WP_016203813.1; NZ_ASRU01000198.1.
DR   AlphaFoldDB; R9C092; -.
DR   PATRIC; fig|1202533.3.peg.3346; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000014030; 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          114..182
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          205..583
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   596 AA;  68725 MW;  2FF6E1F12642C441 CRC64;
     MQLFKTREEV AIFEKWNLGD IYESEEEWEK DLEAVKEKID GLKAFNGKIT NGANLLTYLS
     LSEEVSFIYR KVYAYGMLLL DLDTRNTHAQ SLIEKTRYVG QKYSSATSFF MPYLLSLDEK
     ELKAYIKEEE GLAYFEKDLL ESFRYKKHVL SKEKEEILSE LGESLAVPSN VFGMINNADI
     TFGEVTNDNG EKVELTRGMY AKRIENEDRE VRKEAYLAYY KPYIGLKNTI AATFSAAIKN
     NVKTAKLRNY PSALEKSLFG DQVPVEVYNN LIRTTRKNLP YLDDYMNFRK ERLQIEELHA
     YDLSVPLVGE AAKEEISYDK AFQIMLDALQ PLGEDYISVL KSFKEKRYLD VRETPGKRSG
     AYNLGLYGVH PYILLNHRDD LDSLFTLAHE CGHGMHSYFS SKHQPQISAG YSIFVAEVAS
     TVNEVLLIRH LLKIEKDPDK REHLLHHFID SFKGTFFTQV MFSEFEKTVH EQAENGLPLS
     LDFFNTTYEE LFKAYNGSDL VVDEQVKYGW SRIPHFYRPF YVYKYATGFA SAINIADKLL
     EGKKEDVENY LNFLKSGSSD YPLELLKKTG VDLTTPEPID HALTIFHSLV KEVLGK
//