ID   A0A0Q0VHL4_9SPHI        Unreviewed;       571 AA.
AC   A0A0Q0VHL4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:KQC00210.1};
GN   ORFNames=AQF98_11950 {ECO:0000313|EMBL:KQC00210.1};
OS   Pedobacter sp. Hv1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQC00210.1, ECO:0000313|Proteomes:UP000050543};
RN   [1] {ECO:0000313|EMBL:KQC00210.1, ECO:0000313|Proteomes:UP000050543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hv1 {ECO:0000313|EMBL:KQC00210.1,
RC   ECO:0000313|Proteomes:UP000050543};
RA   Ott B.M., Beka L., Graf J., Rio R.;
RT   "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT   Medicinal Leech Mucosal Castings.";
RL   Submitted (OCT-2015) 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:KQC00210.1}.
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DR   EMBL; LLWP01000005; KQC00210.1; -; Genomic_DNA.
DR   RefSeq; WP_055132199.1; NZ_LLWP01000005.1.
DR   AlphaFoldDB; A0A0Q0VHL4; -.
DR   STRING; 1740090.AQF98_11950; -.
DR   OrthoDB; 9762795at2; -.
DR   Proteomes; UP000050543; 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; cd09606; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011976; Pept_M3B_oligopep-rel.
DR   NCBIfam; TIGR02289; M3_not_pepF; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF48; PUTATIVE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 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:UP000050543};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          174..560
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   571 AA;  65748 MW;  6AF0F17561BAB2CF CRC64;
     MNNLIINKKP RTYIPQDLKI EWENLAPILD ELQKRAINSA QELEQWLKDK SELEAALEED
     FAWRYIKMSC DTANEDLVKS FQYFATEIEP KISPIANELN KKFSESPFID QLDQDKYFVY
     IRAVKKALEL YREENIELFT QLQVAQQKYQ GITGAMSVKI NDQEFTLEQA ANFLKDTNRS
     VRQNAWETIQ QRRLVAKDDL NILFDELVAM RHQVALNAGF ENYRDYMFQA LGRFDYTPKD
     CYDFAEAIEK EVVPVLKEQA EKRQVALGLT TLKPWDMEVS TTGKPALKPF NNGQELIDKS
     IACFTAINPS LGEKLAIMKA NHLFDVESRM GKAPGGYNYP LAETGAPFIF MNSANSLRDL
     TTMVHEGGHA IHTFLTADLA LNDFKHCPSE VAELASMSME LISMDNWDVY FDNEEELNRA
     KKEQLADVLK TLPWVAVIDQ FQHWIYTNPG HNAADREAAF KQIYTRFGAG FADWTDFEQQ
     FGNLWQKQLH LFEVPFYYIE YAIAQLGAIA VWKNYKENPS KALDQYLAAL ALGYTKPMNE
     IYETAGIKFD FSAAYIKELA EFVKDELNKL S
//