ID A0A0K0GCW4_9FIRM Unreviewed; 603 AA.
AC A0A0K0GCW4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=WH51_02240 {ECO:0000313|EMBL:KKE80383.1};
OS Bacilli bacterium VT-13-104.
OC Bacteria; Bacillota; Bacilli.
OX NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE80383.1, ECO:0000313|Proteomes:UP000034981};
RN [1] {ECO:0000313|Proteomes:UP000034981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VT-13-104 {ECO:0000313|Proteomes:UP000034981};
RA Tetz V., Tetz G.;
RT "Bacilli bacterium VT-13-104.";
RL Submitted (APR-2015) 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:KKE80383.1}.
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DR EMBL; LAZH01000012; KKE80383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K0GCW4; -.
DR PATRIC; fig|1637974.4.peg.455; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000034981; 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:UP000034981};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 118..187
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 208..587
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 603 AA; 69713 MW; ABA247C355745D47 CRC64;
MAQSTKQLPK REEVPVEKTW KLEDIFKNDD LWKEEFEQLQ KDIPEITKFQ GKLSESADNL
YNLFKLQDEL GERLGKLYTY AHMRYDQDTT NSFYQALNAK AETVLTLASS SMSYVVPEIL
TMDETKLESF LQEKKELQEY KKVLDEINRQ RPHVLSEKEE VLLAEASEAL STGSQTFSML
NNADLPFPAI KDENGEEIDL THGRYSRFME SKDRRVRKDA FKAMYDTYGQ FKNTFASTLS
GTVKTHNFSA KVRNYDSARQ SALDNNNIPE EVYDNLVEAV NDKLPLLHRY IELRKKVLGV
DELHMYDMYT PLVKDVEMKI SYDEAKDYVI KGLKPLGEEY GKILEQSFEN RWIDVVENKG
KRSGAYSSGA YGTNPYVLLN WQDNVNNTFT LAHELGHSLH SYYTRKNQPY RYGNYSIFVA
EVASTCNEAL LNDYMLKNLE DEKEKLYLLN HFLEGFRGTV FRQTMFAEFE HDIHVQANNG
EALTADKLTE IYYALNKKYY GDAVVSDEEI GLEWARIPHF YYDYYVYQYA TGYSAATALA
NQILTEGDPA VERYLEFLKA GSSDDPIEVL KKAGVDMTSK QPILGALDVF EEKLNEMEKL
LLN
//