ID   W0GKD6_9MOLU            Unreviewed;       602 AA.
AC   W0GKD6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=P344_00900 {ECO:0000313|EMBL:AHI57553.1};
OS   Spiroplasma mirum ATCC 29335.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=838561 {ECO:0000313|EMBL:AHI57553.1, ECO:0000313|Proteomes:UP000019260};
RN   [1] {ECO:0000313|EMBL:AHI57553.1, ECO:0000313|Proteomes:UP000019260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMCA {ECO:0000313|EMBL:AHI57553.1,
RC   ECO:0000313|Proteomes:UP000019260};
RA   Landry C.A., Bastian F.O., Thune R.L.;
RT   "Complete genome sequence of Spiroplasma mirum suckling mouse cataract
RT   agent.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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; CP006720; AHI57553.1; -; Genomic_DNA.
DR   RefSeq; WP_025316974.1; NZ_CP006720.1.
DR   AlphaFoldDB; W0GKD6; -.
DR   STRING; 838561.P344_00900; -.
DR   KEGG; smia:P344_00900; -.
DR   KEGG; smir:SMM_0146; -.
DR   PATRIC; fig|838561.3.peg.173; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_14; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000019260; 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   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:UP000019260};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          108..174
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          205..577
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   602 AA;  69706 MW;  E6419B1DBA41A322 CRC64;
     MKRNEAPAQY KWDFTNLYPT IDDWKKDLNI IVEKLKEIIA FKGKLNNKDI FKKYLQLDDE
     IDLIVSKLGQ YLHMGDIDTT NLVYQELSGI FANTINELSS QLAFISPELK AIGEQIIMGW
     IKSDSELQKY EYGYRKFFRE AQHILSERDE EILSLVSRSR GAAYDIYDLL AYADKKPAYV
     NYQGKEQKLT QALYSEITEE TDPLDDQKLR AETAKLFVQH LTDKKHSFAR VYEAILQRSV
     ESVKLRGYKN TLQASLSGDD VTEDIYESLI KYGRQTSHLN VRYNEILKKY FKFNKYYASD
     SRLKLVKNVP SVNKKYSVEE AKNIIRESLK MLGPEYLSQL EIAWSDNRID YFEDTNKRAG
     AYSSGGNGVE PIILMNWDNT ISSVNTLAHE AGHSVHTLLA DANNPRPLSN YPIILAEVAS
     TVNEHLLFDY LYKNAQSDDE KIYLLQNRIE EITGTFFRQI QFADFEWTAH KMVENNKPLD
     ADKLADLFEK ISNDFGSSVF DKYEENSKQY GWTRILHFFN SPYYVYKYAT CIVASFKLYN
     DVLNNNPETL INFLKQGGRK EPLLILKDIG IDYTNEKVYD GLINKLTSLI DNLEALLNKK
     GN
//