ID A0A1H7VZE0_9BACI Unreviewed; 596 AA.
AC A0A1H7VZE0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=SAMN05192533_101198 {ECO:0000313|EMBL:SEM14601.1};
OS Mesobacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=930146 {ECO:0000313|EMBL:SEM14601.1, ECO:0000313|Proteomes:UP000198553};
RN [1] {ECO:0000313|Proteomes:UP000198553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48,IBRC-M 10115,DSM 25386,CECT 8001
RC {ECO:0000313|Proteomes:UP000198553};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOBW01000001; SEM14601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7VZE0; -.
DR STRING; 930146.SAMN05192533_101198; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000198553; 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:UP000198553};
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 203..582
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 596 AA; 68690 MW; CB25A2DFB39B4505 CRC64;
MTTFKNRTEV PEQEKWNLAD IYSDLAQWEE DYRQIKIMGE SLKQYDGGIH DGSSLYHYLK
LREELSFLFG KVFAYAMLKV DEDTRVTGSQ SYLDRARQLS VKVSSSTSFF MPFLLSLSEE
TLKEYIASEE GLKYFEEDLM ESFRYKSHVL SKEQESILSQ LGEALSVPSQ AFGMINNADI
KFGEVTGEDG EKIELTRGMY SKLIEDEDRE TRQEAYKAYY QPYLGMKNTI ATTLSSAIKN
NVTTARLRQY PSALEKGLFG DKVPREVYEN LIQTTKKHIA PMHQYTRIRK KKLGLQELRQ
YDLSVPLVSG VKQVISYDEA FETMCDALAP LGNEYIEILM TFKKERYLDV RETPGKRSGA
YNLGVYGVHP YILLNHQDDL DSLFTLTHEC GHGVHSWLSS KHQPQITAHY SIFVAEVAST
VNEVLLIQYL LKKENDSQVR KHLLNHFIDQ FKGTFFTQVM FAEFEKKTHE LAEAGAPLNV
EVFNKIYEEL FREYNGDEIV LDEEVKYGWS RIPHFYRPFY VYKYATGFAA AIHIATKLLE
GDENTLSNYL DFLKSGSSDY PLELLKKTGV DLTTPEPIEN ALKKFTELVE AFSEEI
//
