ID   A6TUL8_ALKMQ            Unreviewed;       592 AA.
AC   A6TUL8;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   OrderedLocusNames=Amet_3767 {ECO:0000313|EMBL:ABR49886.1};
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR49886.1, ECO:0000313|Proteomes:UP000001572};
RN   [1] {ECO:0000313|Proteomes:UP000001572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX   PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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; CP000724; ABR49886.1; -; Genomic_DNA.
DR   RefSeq; WP_012064846.1; NC_009633.1.
DR   AlphaFoldDB; A6TUL8; -.
DR   STRING; 293826.Amet_3767; -.
DR   MEROPS; M03.007; -.
DR   KEGG; amt:Amet_3767; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000001572; 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:UP000001572};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          110..178
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          199..579
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   592 AA;  68444 MW;  C0F25D4C8B59C12A CRC64;
     MNKSEIQEQY RWDLSDLFTS DDEWEEAFKA VRENAEAFKG FKGRILESPE RLYEAIKEHE
     KVSRMITNVL TYARLRKDEN TKNATYQSMT ARAEKLATEI SEMGSFFTPE ILSAAYETIK
     EMSLYPPLKM YEQFFEDLFR SKKHTLSEEM ESVLAQVGEL GDVPSNTYGM LLNADMTFED
     AVDAKGDPHK LTNGSYIQLM MSADRTLRQD AFGKYYKVYE GHINTIATLL QSEVNKNIFF
     SKVRKHPSAR EAALFQNNIP TSVPDQLIEA VNANLETFYK YMKLRKKVLG LDELHLYDIY
     RPIVTNVDFD IPYEEAKTMV TESLGLLGEN YQKTIREAFE QRWIDVYETE GKRSGAYSWG
     TYDSKPYILL NHKDNIDSMF TLTHELGHSM HSYLTRENQP YVYGNYSIFL AEVASTTNEA
     LLNDYLLKNI HDEDKKKYIL NHYLEQFRGT IFRQTMFAEF ERDIHDHVEK GGALTAEFLC
     DHYLNLNKKY FGPDVVIDDA IKYEWARIPH MYYNFYVYQY ATGFSAAIAL SNAILKEGEP
     AVKCYTEFLS SGSKDYPIDI LRKAGADMET EAPVNNALAL FTSAVEELEA LL
//