ID K6S0B8_LACPA Unreviewed; 603 AA. AC K6S0B8; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 25-MAY-2022, entry version 32. DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091}; DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091}; GN ORFNames=LCAUCD174_0758 {ECO:0000313|EMBL:EKQ21323.1}; OS Lacticaseibacillus paracasei (Lactobacillus paracasei). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lacticaseibacillus. OX NCBI_TaxID=1597 {ECO:0000313|EMBL:EKQ21323.1, ECO:0000313|Proteomes:UP000001348}; RN [1] {ECO:0000313|EMBL:EKQ21323.1, ECO:0000313|Proteomes:UP000001348} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD174 {ECO:0000313|EMBL:EKQ21323.1, RC ECO:0000313|Proteomes:UP000001348}; RX PubMed=23035691; DOI=10.1186/1471-2164-13-533; RA Broadbent J.R., Neeno-Eckwall E.C., Stahl B., Tandee K., Cai H., RA Morovic W., Horvath P., Heidenreich J., Perna N.T., Barrangou R., RA Steele J.L.; RT "Analysis of the Lactobacillus casei supragenome and its influence in RT species evolution and lifestyle adaptation."; RL BMC Genomics 13:533-533(2012). 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:EKQ21323.1}. 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; AFYQ01000034; EKQ21323.1; -; Genomic_DNA. DR RefSeq; WP_003593616.1; NZ_AFYQ01000034.1. DR EnsemblBacteria; EKQ21323; EKQ21323; LCAUCD174_0758. DR PATRIC; fig|1051659.3.peg.791; -. DR Proteomes; UP000001348; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd09609; M3B_PepF; 1. DR Gene3D; 1.10.1370.20; -; 1. DR InterPro; IPR034009; M3B_PepF_4. 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 PANTHER; PTHR11804; PTHR11804; 1. DR Pfam; PF01432; Peptidase_M3; 1. DR Pfam; PF08439; Peptidase_M3_N; 1. DR TIGRFAMs; TIGR00181; pepF; 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 116..182 FT /note="Peptidase_M3_N" FT /evidence="ECO:0000259|Pfam:PF08439" FT DOMAIN 203..584 FT /note="Peptidase_M3" FT /evidence="ECO:0000259|Pfam:PF01432" SQ SEQUENCE 603 AA; 68044 MW; 2253067402DC101A CRC64; MSETALPKRQ EVDPKLTWDL TPIFADEFAY TEAIKQVRAL TKDFVHLYQG KLTEPAIIVD ALGDYGSIIE LDSKIGHWAF MPYSTDTTDP KLRDRQIKAT ALDGEIGGQL SFFQAELTQL PEEVLDAVVA KAPDYAGFFR QIKIAKKGAL APAAEKVLAE LSPVFQAPSN IRDQTIFGDM DFGTFTAHGK TYPLSFVMYE ENYQKHPDTE VRRAAYAKFN QTLRRYQNTM AAGYLAQVTR EKITATMRGY DSVIDYLLAD QEVSRAMFDR QIDVIMHDLA PIMRKYITHV KELWGLDHIG YTDLQIDIDP AYSPTITLDQ AKQDIEQATA IMGHDYQAQM MQAFTDHWID FPANQGKDSG AYTAGPYGVH PYVEMTWSNS LPAVYTLIHE LGHTAQMVRS EKAHNILDAD FNDYLVESPS TFNELLLTHY LDQTAKDPQM KRFALSRLLN DTYFHNFVTH LLEAAFQRKV YQRIDAGDSF DAAELNAIKR QVLTDFWGPA VELEEGAELT WMRQSHYYMG LYSYSYSAGL MVATQAFQAI EQQGQPAVDR WLRYLSLGDS LNPVAAARVA GVDVTTDAAL KQTIAFLGRT VDEIISLSHE ING //