ID   Q6E3K7_9ACTN            Unreviewed;       452 AA.
AC   Q6E3K7;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative proline peptidase {ECO:0000313|EMBL:AAT47517.1};
GN   Name=pcfC {ECO:0000313|EMBL:AAT47517.1};
OS   Propionibacterium freudenreichii.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=1744 {ECO:0000313|EMBL:AAT47517.1};
RN   [1] {ECO:0000313|EMBL:AAT47517.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMGT 2946 {ECO:0000313|EMBL:AAT47517.1};
RX   PubMed=15574930; DOI=10.1128/AEM.70.12.7303-7310.2004;
RA   Brede D.A., Faye T., Johnsborg O., Oedegaard I., Nes I.F., Holo H.;
RT   "Molecular and genetic characterization of propionicin F, a bacteriocin
RT   from Propionibacterium freudenreichii.";
RL   Appl. Environ. Microbiol. 70:7303-7310(2004).
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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; AY587566; AAT47517.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6E3K7; -.
DR   ESTHER; 9acto-q6e3k7; AlphaBeta_hydrolase.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          34..178
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          372..439
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   452 AA;  48433 MW;  EC532C46A4A516D3 CRC64;
     MAIPRISISG VKKNPRAKIK IHRAASNSGS KGTIFYNPGG PAISAVDTLK DLVSFLDPRI
     VNDNDIVAID PIGVGDSDGV VCITPSLPEQ HYGVLPSNYV EFKDHLNNVD PIISRTCSSE
     FAMGSIAQAR DIEYIRVALG LKSVTFLGVS YGSILATVYA KLYPRSVSSL IVDSPVDPYS
     SYQSNGQGIW ARIGIPATSQ EALMSAIGLC ESIGIGRCPV ALTIRSSFER VMNRLQVSTI
     NAGKGRAVDL SSFESYVSAR LYHFNSLGID DFELLFDQII QLANASELGT GAEPPVAVDD
     VGLTDLIIRL SRMNLVLCSD YPQIDNALLP ADAMISELKS PGSGYYYAAM TSSCRNGDRG
     QGRVGGLLQS GPQLPRTIVF ENSHDPVSST QAAVHVKNMS SRASVVTVSD WWGHGALRAS
     KCTNEELYAF LRGGRGPFSG SRVCAPNQAM FP
//