ID Q5FIA0_LACAC Unreviewed; 598 AA.
AC Q5FIA0;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN Name=pepF {ECO:0000313|EMBL:AAV43574.1};
GN OrderedLocusNames=LBA1763 {ECO:0000313|EMBL:AAV43574.1};
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621 {ECO:0000313|Proteomes:UP000006381};
RN [1] {ECO:0000313|EMBL:AAV43574.1, ECO:0000313|Proteomes:UP000006381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM
RC {ECO:0000313|Proteomes:UP000006381};
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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}.
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DR EMBL; CP000033; AAV43574.1; -; Genomic_DNA.
DR RefSeq; WP_003549813.1; NC_006814.3.
DR RefSeq; YP_194605.1; NC_006814.3.
DR AlphaFoldDB; Q5FIA0; -.
DR STRING; 272621.LBA1763; -.
DR MEROPS; M03.007; -.
DR GeneID; 56943323; -.
DR KEGG; lac:LBA1763; -.
DR PATRIC; fig|272621.13.peg.1683; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_9; -.
DR OrthoDB; 9766487at2; -.
DR BioCyc; LACI272621:G1G49-1730-MONOMER; -.
DR Proteomes; UP000006381; Chromosome.
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:UP000006381};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 113..181
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 203..583
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 598 AA; 68255 MW; E37B5A33BC2F2C4E CRC64;
MAIPTRSEVP EELKWDLTRV FKTDEDWEAA FDNAKDEVEK LGDFKKILTK SGKDLYESLT
QILAVKRQVE NIYVYATMSS DVDTSNSHYL GYVSRAQNLV NQFEAVTSFI SPEILSIPAD
KFEQFKKDEP RLNDYAHYLE TITNKRPHTL PAEEEKIIAD ASDAMGVSEN TFNVLTNSDM
EYGYVQDDDG NMEQLSDGLY SLLIQSQNRD VRKGAFDTLY ASYGQFQNSL ASTLSGVVKK
HNYNAKVHKY DSAREAALAE NNVPTKVYDT LIREVDSHLD LLHRYVALRK KILGLKDLQM
WDMYVPLTGK PALSYNFEEA KEVAKKALAP LGEDYLKHVD YIFNNRVIDV VESKNKVTGA
YSGGAYDTDP YELLNWENNI DSLYTLVHET GHSVHSWYTR NSQPYVYGDY PIFVAEIAST
TNENILTEYF LDHITDSKTR AFILNYYLDS FKGTLFRQTQ FAVFEQFIHE ADAKGEPLTA
DILDEVYGQL NQHYYGDSVE PGGDIALEWS RIPHFYYDFY VYQYATGFAA ATALANKVVH
GSEADRDAYL GFLKAGSSNY PTEIMKHAGV DMTKPDYLED AFKTFEKRLA EFESLIEK
//
