ID A0A0Q3WKT1_9BACI Unreviewed; 598 AA.
AC A0A0Q3WKT1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=AN964_24650 {ECO:0000313|EMBL:KQL50812.1};
OS Heyndrickxia shackletonii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL50812.1, ECO:0000313|Proteomes:UP000051888};
RN [1] {ECO:0000313|EMBL:KQL50812.1, ECO:0000313|Proteomes:UP000051888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL50812.1,
RC ECO:0000313|Proteomes:UP000051888};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-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}.
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:KQL50812.1}.
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DR EMBL; LJJC01000015; KQL50812.1; -; Genomic_DNA.
DR RefSeq; WP_055742419.1; NZ_LJJC01000015.1.
DR AlphaFoldDB; A0A0Q3WKT1; -.
DR PATRIC; fig|157838.3.peg.5424; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000051888; Unassembled WGS sequence.
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 Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 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:UP000051888};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 114..182
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 203..583
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 598 AA; 68653 MW; 9A66143A243CF888 CRC64;
MTIYASRQEI PEKEKWNLTD IYPTVEDWNK DVQYIEQAAE ELKKFDGNIH DGKALLSYLT
ENEKVSFKFG KVYAYSMLSV DLDTRDTASQ SLQDKAKQVG VKVSSATSFF MPFLLGLEET
TLKAYMEEEK GLQYFEKDLH DAYRYKAHVL SKEKEEVLSQ LGEALSAPSH TYGMMNNADI
KFGKVTKADG EKVELTRGMY AKLIEDQDRN KRKEAYKAYY QPYVHLKNSI ASTLGAAIKN
NVTVSRLRHY PSALEKALFA DNVPKEVYDN LISATKQNIE PLHRYAEIRK EKLGLDELHQ
YDLNVPLVEG VEKEISFDEA YKTMLDALRP LGDDYINTLA SFKEARYIDV RETPGKRSGA
YNLGVYGVHP YVLLNHRDNI DGLFTLAHEM GHAMHSHYSH KTQPQNTAKY SIFVAEVAST
VNEVLLINYL LNKETDEKLR QYLLNHFIDK FKGTLFTQVM FGEFEKITHE LAEKGEPLNA
KVFSEVYENL FREYNGDQIV FDEEVKYGWS RIPHFYRPFY VYKYATGFAS AVHIANRILD
GDSKTQAAYL EFLKSGSAEY PLDLLKKTGV DLTSPEPVEK ALKQFSELVE EFAKIPIK
//
