ID R5IPR7_9CLOT Unreviewed; 594 AA.
AC R5IPR7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=BN757_00547 {ECO:0000313|EMBL:CCY44178.1};
OS Clostridium sp. CAG:7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262832 {ECO:0000313|EMBL:CCY44178.1, ECO:0000313|Proteomes:UP000018268};
RN [1] {ECO:0000313|EMBL:CCY44178.1, ECO:0000313|Proteomes:UP000018268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:7 {ECO:0000313|Proteomes:UP000018268};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY44178.1}.
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; CAYE010000167; CCY44178.1; -; Genomic_DNA.
DR AlphaFoldDB; R5IPR7; -.
DR STRING; 1262832.BN757_00547; -.
DR MEROPS; M03.007; -.
DR Proteomes; UP000018268; 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:UP000018268};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 111..180
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 201..581
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 594 AA; 68309 MW; 8E95B2F8BC3F6C02 CRC64;
MKKRSEAEIS TTWKLEDMVP DNETWEKQLK EASGELEKYG EFKGKLAESA ENLYQCLKFD
DEFSLKAERL YVYARMRSDE DTANDLYQDM FSRAQLLNIR ASENSSYMVP EILSIPEEIL
KEYRSSHPGL KHFDRLLDQL LERKSHTLSK EMEQLLAQSY EATQGGSQVF TMFNNADARF
PAVHDAEGKE IPLTHGNYIA LLENQNRDIR KEAFENLYSV YKQFSNTLSA AFGANVKQAV
FYAKARNYTS SRQASLSGNE VPESVYDNLV ASVRKSLPLL HRYVSLRKKL LGVEELHMYD
LYVPMVAEAD RHYTFEEAKD IVKTGLAPMG EEYLGLLQEG FDNRWIDVYE NEGKRSGAYS
WGVYGCHPYV LLNFHGTLND VFTLAHEMGH SIHTWYSNKN QSYTYSGYKI FVAEVASTCN
EALLIRHLLK NSKDKQEKAY LLNYFLESFR GTLFRQTMFA EFEQKAHEMA AAGESMTSQS
LCNIYKKLNE DYFGPDTVID PEIQYEWERI PHFYTPFYVY QYATGFSAAI AISRKIFNGE
LGILEGYKKF LSGGCSDTPI ELLKLAGVDM SHTGPVEEAL KFFEELLNEF EELA
//
