ID A0A0R1S529_9LACO Unreviewed; 601 AA.
AC A0A0R1S529;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=FC85_GL001540 {ECO:0000313|EMBL:KRL63737.1};
OS Lentilactobacillus diolivorans DSM 14421.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423739 {ECO:0000313|EMBL:KRL63737.1, ECO:0000313|Proteomes:UP000052013};
RN [1] {ECO:0000313|EMBL:KRL63737.1, ECO:0000313|Proteomes:UP000052013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14421 {ECO:0000313|EMBL:KRL63737.1,
RC ECO:0000313|Proteomes:UP000052013};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRL63737.1}.
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DR EMBL; AZEY01000101; KRL63737.1; -; Genomic_DNA.
DR RefSeq; WP_057865907.1; NZ_AZEY01000101.1.
DR AlphaFoldDB; A0A0R1S529; -.
DR STRING; 1423739.FC85_GL001540; -.
DR PATRIC; fig|1423739.3.peg.1613; -.
DR Proteomes; UP000052013; 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:UP000052013};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 117..186
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 207..588
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 601 AA; 69092 MW; E96969F3C682BAEE CRC64;
MAKAKELPLR KDVPVQLTWD LTTVYKNDDA FETDFNEIEK ELVPVKKLAG SLSEGAGQLL
KATEFILAVN RKLEKVYVYA QLKNDQDTSD DKYQAMFARC ESLAAQFGAA MAWFDPELLQ
LSEKTMSKYY QDEPKLKAFK RLFDQTFEKR DHILGNDVEE VLAGAGDIFS SGEKTFGILD
NTDLSFPVVT DENGKQVKLS QGVYAILLES ADQNIRKQAF EKLYEVYDQF QHTLAATLTT
NVKNHNFKAK IRKYHNALQA ALSANEVPTV VYDNLIKVVN EHLDLLHRYV ALRKKILGVD
ELHMYDLYTS LIGKKSPRYT FDQSKQIALE ALQIMGPDYV SHVKEEFDNR WVDVVENQFK
RSGGYSSGTY DTNPFILLNW KDNLDNLYTL IHGTGHSMHS YYAHHNQPYQ TGDYSIFVAE
IASTTNENIL TDYLLNKFKN NDEMKKQILN YYLDGFKGTV FRQTQFAEFE QFIHEQDASG
RPLTANFMND YYLSLNQKYY GDAVVSDRQI GLEWSRIPHF YYNFYVYQYA TGFAAASTLA
DNIVNGDSSN VEKYLNYLKS GSSDIPTNVM KKAGVDMTKP EYLEKAFAIF ENRLDEFEKL
F
//
