ID   A0A0S7ZEZ4_9BACT        Unreviewed;       610 AA.
AC   A0A0S7ZEZ4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Oligoendopeptidase F {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMJ57_04285 {ECO:0000313|EMBL:KPJ85115.1};
OS   Parcubacteria bacterium SG8_24.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1703768 {ECO:0000313|EMBL:KPJ85115.1, ECO:0000313|Proteomes:UP000051503};
RN   [1] {ECO:0000313|EMBL:KPJ85115.1, ECO:0000313|Proteomes:UP000051503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_24 {ECO:0000313|EMBL:KPJ85115.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPJ85115.1}.
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DR   EMBL; LJNP01000035; KPJ85115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7ZEZ4; -.
DR   STRING; 1703768.AMJ57_04285; -.
DR   PATRIC; fig|1703768.3.peg.843; -.
DR   Proteomes; UP000051503; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09610; 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; IPR001567; Pept_M3A_M3B_dom.
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|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          112..181
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          337..588
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   610 AA;  68855 MW;  3DCD272FC0EE998E CRC64;
     MAKKETGAEN VRWDLGCFYR SIDDPQIEQD VKWYITRAEL FESDYRGKLG EALGRAIQAR
     AELSMLGSKI GYFLFLSFCT DLNDEKVKSK MNGIEDRMQH AAGKHLAWVA NEMCDLDQAV
     IDAAIESDPV VAHHRSWIED IRKDKPHLLS TEVESALAMR SPFSSSSWSE FFDEVEADLR
     FPLDDEEHTM EEILDIMSYD PDSDRRARAL KVIHDVFGGH FIKYSAQTLG LVVRENALEN
     KERNYPHPMA SRNIDNKVSD GIVEALHQAV KEAAGPLAVR HYRLKARLLG KERLLWSDRN
     AKPPFADTSV IPYQEAERMV LKAYRSFSPT LAELVQSMID LRRIDAPVVK GKRSGAFCCY
     TMVPGQVPIS YVLLNYLGTT RDVMTMAHEL GHAVHGLLGY ETQGILMGSA PTAYAETASI
     FGEMTTFNAL KARLLEQGDE RSLLALLMDK ADGAINSVVR QIGFSNFERQ VHGRVHEGGG
     WPTIEELNGL WMGTVKELYG EDGDVFDYRD TERLWCYIPH FHDPFYVYAY ACGELLTQSL
     YALQGELKER FEPLYLEMLK SGGTKSLKGL LAPFGQDPED PQFWANGIRI SLGKMVDEAE
     SLAKRLDLIP
//