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Database: UniProt
Entry: A0A0R1WYA5_9LACO
LinkDB: A0A0R1WYA5_9LACO
Original site: A0A0R1WYA5_9LACO 
ID   A0A0R1WYA5_9LACO        Unreviewed;       594 AA.
AC   A0A0R1WYA5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Oligoendopeptidase F2 {ECO:0000313|EMBL:KRM19795.1};
GN   ORFNames=FC40_GL001314 {ECO:0000313|EMBL:KRM19795.1};
OS   Ligilactobacillus hayakitensis DSM 18933 = JCM 14209.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1423755 {ECO:0000313|EMBL:KRM19795.1, ECO:0000313|Proteomes:UP000051054};
RN   [1] {ECO:0000313|EMBL:KRM19795.1, ECO:0000313|Proteomes:UP000051054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18933 {ECO:0000313|EMBL:KRM19795.1,
RC   ECO:0000313|Proteomes:UP000051054};
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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:KRM19795.1}.
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DR   EMBL; AZGD01000031; KRM19795.1; -; Genomic_DNA.
DR   RefSeq; WP_035520296.1; NZ_BAML01000049.1.
DR   AlphaFoldDB; A0A0R1WYA5; -.
DR   PATRIC; fig|1423755.3.peg.1393; -.
DR   eggNOG; COG1164; Bacteria.
DR   OrthoDB; 9769691at2; -.
DR   Proteomes; UP000051054; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09607; 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   InterPro; IPR034006; M3B_PepF_2.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   NCBIfam; TIGR02290; M3_fam_3; 1.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051054};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          110..176
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          192..574
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   COILED          20..54
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   594 AA;  67542 MW;  02D158538E4A35C5 CRC64;
     MKEYSEVWDL ESIFAGGSNS AAFQERLEKL KVEIKELEEK ISTWQADAAG LKEILAVMTK
     VDEGLSQLGA FAEALSSADV TDSQALQLDS QVMALIPEYS QVNKEFQRSL AQIPDEKWES
     LLEDSDLKSV AFVLGEFRRD GANFLSAAEE NIIAQLKLDG QTAWSRHYDV LSGNLKVEHD
     NKQLSAGQAF NLMMASKDNE VRDQLFEKWE EAWGKDEQLY ADTLNHIDGA RLTDQKLHGN
     TDYLKEPREY NRLKQETLDQ MWAVVAKNKQ SFVEYMNRKA QLLGRQKPVW QDQEAPVVLG
     DFEAKHYTFS QAAEFIMENF EKFSPKMAAL AKKAFEGQWI EAQDRPNKRA GGYCTGFPEN
     QESRIFMTFG GSVNEVATLA HELGHAFHSS VMWDLPHLNQ GYAMNVAETA STFAEQVVND
     AAIASVTSKE EKINLLDQKL QGALAMFFNI HARYIFERSF YEARQTKVLS PKEISDLMVK
     AQKEAFADSL ANWHPHFWAA KLHFYIDDVP FYNFPYTFGY LFSQGIYAQA KKVGGSFEDQ
     YIALLRDTGA MTTEELAQKH LGVDLTKADF WQAGIDTILE DVKEFMELTE EYVK
//
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