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Database: UniProt
Entry: A0A0R1UC23_9LACO
LinkDB: A0A0R1UC23_9LACO
Original site: A0A0R1UC23_9LACO 
ID   A0A0R1UC23_9LACO        Unreviewed;       598 AA.
AC   A0A0R1UC23;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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=FC46_GL001539 {ECO:0000313|EMBL:KRL90929.1};
OS   Lactobacillus kalixensis DSM 16043.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423763 {ECO:0000313|EMBL:KRL90929.1, ECO:0000313|Proteomes:UP000051036};
RN   [1] {ECO:0000313|EMBL:KRL90929.1, ECO:0000313|Proteomes:UP000051036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16043 {ECO:0000313|EMBL:KRL90929.1,
RC   ECO:0000313|Proteomes:UP000051036};
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:KRL90929.1}.
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DR   EMBL; AZFM01000005; KRL90929.1; -; Genomic_DNA.
DR   RefSeq; WP_057797602.1; NZ_AZFM01000005.1.
DR   AlphaFoldDB; A0A0R1UC23; -.
DR   STRING; 1423763.FC46_GL001539; -.
DR   PATRIC; fig|1423763.3.peg.1563; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000051036; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          112..180
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          202..582
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   598 AA;  68084 MW;  CF423004F0D911F4 CRC64;
     MAIPARNEVP EELKWDLTRV FKDDQEWENE FENVKNDIAD LSSLKGSFTS GKALYEGLTQ
     MLGVSRRLEK VYVYATMSSD VDTADAHYLG YVARVQSLTA QFEAATSFTN PEILAIPAEE
     LEKFKQDEPR LKDYDHLLEV ITKKRPHTLP AEQEKIIADA SDALNVSAST FNVLTNSDME
     YGYVQDENGE MVQLSDGLYS LLIQSQDRKV RKNAFDVMYA SYGQFENSLA STLSGNVKAH
     NFNAKAHKFD SARDAALAEN NVPTVVYDTL IKEVDSHLDL LHRYVNLRKK ILGLKDLQMW
     DMYVPLTGKP ALTYTFEEAK EEAKKALAPL GEDYLKHVDY IFNNRIIDVV ESKNKVTGAY
     SGGSYDTDPY ELLNWENNVD SLYTLVHETG HSVHSWYTRN TQPYAYGDYP IFVAEIASTT
     NENILTEYFL DHITDPKTRA FVLNYYLDAF KGTLFRQAQF AEFEQFIHEA DAKGQPLTAD
     ILDKFYGDLN QRYYGDSVEE GGDIAKEWAR IPHFYYNFYV YQYATGFAAA AALSDKIVHG
     SDEDREKYLG FLKAGSSDYP VEIMKNAGVD MTKPDYLEAA FASFEKRLDE FEKLIGKF
//
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