ID V8CJJ0_9HELI Unreviewed; 600 AA.
AC V8CJJ0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Oligoendopeptidase F {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF2087_00171 {ECO:0000313|EMBL:ETD27262.1};
OS Helicobacter canis NCTC 12740.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1357399 {ECO:0000313|EMBL:ETD27262.1, ECO:0000313|Proteomes:UP000018688};
RN [1] {ECO:0000313|EMBL:ETD27262.1, ECO:0000313|Proteomes:UP000018688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12740 {ECO:0000313|EMBL:ETD27262.1,
RC ECO:0000313|Proteomes:UP000018688};
RG The Broad Institute Genomics Platform;
RA Earl A., Fox J.G., Shen Z., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Helicobacter canis NCTC 12740.";
RL Submitted (OCT-2013) 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}.
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:ETD27262.1}.
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DR EMBL; AZJJ01000001; ETD27262.1; -; Genomic_DNA.
DR RefSeq; WP_023929067.1; NZ_KI669458.1.
DR AlphaFoldDB; V8CJJ0; -.
DR STRING; 1357399.HMPREF2087_00171; -.
DR PATRIC; fig|1357399.3.peg.175; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_3_0_7; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000018688; 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; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000018688};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 120..185
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 200..575
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 68951 MW; 06F3B5C92A6475FE CRC64;
MAKPHKHNTL HKSPKSKETP HNWDLSALFA DNEQASQYLA TTYKQAKAFQ EHYQNTLATL
TPKDFYTALL AYEQLIERIS RVMTYAFLLF AQDTKKGDIY AQYELKSNEA HSLLVFFELE
FCELESKVQQ AFIKQAHTHT FYLQTLLQAK PYQLPLSAEQ ALIATSSVGV NAFSRLFDEH
LSALKIGKNK QSEEEVLAEL HSPKRKKRKQ AQKAFTKSLE DSSPLLCYIL NMVRKDVAIT
TKLRGYPSKE APRHLSNHIT QKSVDSMIDI TTKHYHIVQD YYRIKADLMG IKLKDYDRYA
PLFSHASTMH YNQAIELVTQ TYKGFSKEFG TIVEKALQEG WISSHPMPNK RGGAFSHGSV
PSAHPYVLLN WTGNRRDAFT IAHEFGHMIH QELSKKVGTL SHDTPLTTAE TASVFGEMLL
FDHLKSTLSK QELLPIYAGK LEDIFSTLFR QVVMTNFERA IHSKDGELQI ADFDRIWQEE
NAKMFGKSVE LTKNYARWWS YIPHFIHSPF YCYAYSYGQL LVLALFGLYK SGKCKDFVAT
YTEFLSLGGS KAPSELIKAF GFDIESDRFW EIGMQEVRAM LEEFHSLLHA SGYKVRKLKR
//
