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Database: UniProt
Entry: A0A0H3XJ08_9MOLU
LinkDB: A0A0H3XJ08_9MOLU
Original site: A0A0H3XJ08_9MOLU 
ID   A0A0H3XJ08_9MOLU        Unreviewed;       602 AA.
AC   A0A0H3XJ08;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=pepF {ECO:0000313|EMBL:AKM53761.1};
GN   ORFNames=SERIO_v1c01680 {ECO:0000313|EMBL:AKM53761.1};
OS   Spiroplasma eriocheiris.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=315358 {ECO:0000313|EMBL:AKM53761.1, ECO:0000313|Proteomes:UP000035661};
RN   [1] {ECO:0000313|EMBL:AKM53761.1, ECO:0000313|Proteomes:UP000035661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TDA-040725-5 {ECO:0000313|Proteomes:UP000035661};
RX   PubMed=26254485; DOI=10.1093/gbe/evv160;
RA   Lo W.S., Gasparich G.E., Kuo C.H.;
RT   "Found and Lost: The Fates of Horizontally Acquired Genes in Arthropod-
RT   Symbiotic Spiroplasma.";
RL   Genome Biol. Evol. 7:2458-2472(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TDA-040725-5 {ECO:0000313|Proteomes:UP000035661};
RA   Lo W.-S., Kuo C.-H.;
RT   "Complete genome sequence of Spiroplasma eriocheiris TDA-040725-5 (DSM
RT   21848).";
RL   Submitted (JUN-2015) 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; CP011856; AKM53761.1; -; Genomic_DNA.
DR   RefSeq; WP_047791034.1; NZ_CP011856.1.
DR   AlphaFoldDB; A0A0H3XJ08; -.
DR   KEGG; seri:SERIO_v1c01680; -.
DR   PATRIC; fig|743698.3.peg.170; -.
DR   Proteomes; UP000035661; 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:UP000035661};
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          206..577
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   602 AA;  69518 MW;  D56D6145F543C400 CRC64;
     MKRSEAPAQY KWDFTNLYPT IDDWKKDLKI IVEKLKEIIA FKGKLNNKNI FKKYLQLDDE
     IDLIASKLGQ YLHMGDIDTT NLVYQELSGI FANTINELSS QLAFISPELK AIGEQTIMGW
     IKADSDLQKY EYGYRKFFRE AQHILSERDE EILSLVSRSR GAAYDIYDLL AYADKKPAYV
     NYQGKEQELT QALYSEITEE TDPLNEQKLR AETAKLFVQH LTDKKHSFAR VYEAILQGSV
     ESVKLRGYKN TLQAALSSDD VTEDIYESLI KFGRQTSHLN VRYNEILKKY FKFNKYYASD
     SRIKLVKNVP SVNKKYSVEE AKNIIRESLK MLGPEYLSQL EIAWSDYRID YFEDTNKRAG
     AYSSGGNGVE PIILMNWDNT ISSVNTLAHE AGHSVHTLLA DANNPRPLSN YPIILAEVAS
     TVNEHLLFDY LYKNAQSDDE KIYLLQNRIE EITGTFFRQI QFADFEWTAH KMVENNEPLD
     ADKLADLFEK ISNDFGSSVF DKYEENSKPY GWTRILHFFN SPYYVYKYAT CIVASFKLYN
     DVLNNNSATL INFLKQGGRK EPLLILKDIG IDYTDEKVYD GLINKLTSLI DDLETLLNKK
     GN
//
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