ID G2M3C9_HELPX Unreviewed; 578 AA.
AC G2M3C9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:AEN15084.1};
GN ORFNames=HPPN120_02275 {ECO:0000313|EMBL:AEN15084.1};
OS Helicobacter pylori Puno120.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1055528 {ECO:0000313|EMBL:AEN15084.1, ECO:0000313|Proteomes:UP000008532};
RN [1] {ECO:0000313|EMBL:AEN15084.1, ECO:0000313|Proteomes:UP000008532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puno120 {ECO:0000313|EMBL:AEN15084.1,
RC ECO:0000313|Proteomes:UP000008532};
RA Kersulyte D., Cabrera L., Hooper C.C., Jahuira Arias H., Gilman R.H.,
RA Berg D.E.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP002980; AEN15084.1; -; Genomic_DNA.
DR RefSeq; WP_000662815.1; NC_017378.1.
DR AlphaFoldDB; G2M3C9; -.
DR KEGG; hep:HPPN120_02275; -.
DR PATRIC; fig|1055528.4.peg.453; -.
DR HOGENOM; CLU_021290_3_0_7; -.
DR Proteomes; UP000008532; Chromosome.
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; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 103..168
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 184..560
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT COILED 8..35
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 578 AA; 67687 MW; BC335CCFA80F32C0 CRC64;
MKEQEWDLSA LFENKESAEE FLKTLQTEAQ EFESAYQNNL KSLDATKFAN ALKHYENLSE
KISKVMTYAQ LLFAKNTKEA KFYSQCEMAC TNIQQHLLFF EIEFKNLDAK KQLAFIKKCK
NHAFYLNNLI ERKKHTLNLD EEKIALALSP VGVGAFSRLF DEHFSSLKIP FEEQNLSEEE
ILALLHNPKR KIRKKSQKAF SKALEKSRPL LTYILNMVRK DLLIETRLRK YDKKESFRHI
DNQISQESVD SMIEIVNANF SLVHRYYHQK AQILGHKLKD YDRYAPLSDE HTTMTYSQAL
GEVLNTLKAF SPEFHKIASK AIKEGWVDSH PKDFKQGGAF SHGGVPSAHP YVLLNYTGNR
RDAFTIAHEF GHMIHQELSK KQGVLNMDTP LTTAETASVF SEMLFFEHLK KGLKSDELLF
MLAGKLEDIF STLFRQVVMT NFERRIHEID EELDTKDFDR IWFEENQRMF EKSVKLTKNY
HLWWSYIPHF IHSPFYCYAY SYGQLLTLAL YGLYKKSDAK EFVKTYTEFL SLGGSKSPKE
LVSMFGFDID SKEFWEIGMQ EVRHLLEEFE RLLACKEN
//
