ID   A9NG69_ACHLI            Unreviewed;       598 AA.
AC   A9NG69;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   OrderedLocusNames=ACL_0733 {ECO:0000313|EMBL:ABX81349.1};
OS   Acholeplasma laidlawii (strain PG-8A).
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX81349.1, ECO:0000313|Proteomes:UP000008558};
RN   [1] {ECO:0000313|EMBL:ABX81349.1, ECO:0000313|Proteomes:UP000008558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-8A {ECO:0000313|EMBL:ABX81349.1,
RC   ECO:0000313|Proteomes:UP000008558};
RX   PubMed=21784942; DOI=10.1128/JB.05059-11;
RA   Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA   Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA   Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA   Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA   Ladygina V.G., Govorun V.M.;
RT   "Complete genome and proteome of Acholeplasma laidlawii.";
RL   J. Bacteriol. 193:4943-4953(2011).
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; CP000896; ABX81349.1; -; Genomic_DNA.
DR   RefSeq; WP_012242680.1; NC_010163.1.
DR   AlphaFoldDB; A9NG69; -.
DR   STRING; 441768.ACL_0733; -.
DR   GeneID; 66293726; -.
DR   KEGG; acl:ACL_0733; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_1_1_14; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000008558; 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; cd09609; 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; IPR034009; M3B_PepF_4.
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; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 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:UP000008558};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          115..181
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          204..583
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   598 AA;  69133 MW;  5370B895AA04EB41 CRC64;
     MKKQLPKRSE IDIKHTWDVH SIYKDDQAFN QTFDTLEGLV KEFVVKYEKR LTDAHIITSS
     LNDLKVINEM ITSLSAYASL QSSVDGVDEA NQMRSGKTSI RLQKVSKQLN FFHSELNKVT
     KKVLMDAMRI DESNKLYLED VLEYKKHTLK PEAEKLLNAL SPVLNAPYGS YNRFKLVDMK
     FSDFEVDGQT YPNSFTLFEN EYEYDGNTKV RRKSYEAFYS KLSEYQHGFA SQYYAQLQKE
     KALADARGFK SVFDYLLYSQ KVPKSFMDRQ IDVIMKDLAP AMRKYAKHLG KLHGLDQVTY
     ADLKIAVDDS FEPKVTIESS KELLMDGLSI LGEDYLEIVR RSFDERWIDF PQNVGKSTGG
     FCSSPYGQNS FILINWNGQM DEVMVLAHEI GHAGHFQYAN KYQNIFNTRP SLYFIEAPST
     TNELIMARHL MKHATDARTK RWIQSVMISR TYYHNFVTHL LEAAFQRKVY EKIDNYEPIS
     ASVLNNIKLD VLRQFWGDAV VIPDYAGLTW MRQPHYFMGL YPYTYSAGLT LGTVVSQRIF
     EKTLDPKDWI EVLKAGATKK PLDLALMVDV DLKTSKPLKE AIKFISQTID EIIAYDKK
//