ID A0A073K810_9BACI Unreviewed; 595 AA.
AC A0A073K810;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=BAGA_17145 {ECO:0000313|EMBL:KEK22691.1};
OS Bacillus gaemokensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574375 {ECO:0000313|EMBL:KEK22691.1, ECO:0000313|Proteomes:UP000027778};
RN [1] {ECO:0000313|EMBL:KEK22691.1, ECO:0000313|Proteomes:UP000027778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15801 {ECO:0000313|EMBL:KEK22691.1,
RC ECO:0000313|Proteomes:UP000027778};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus gaemokensis JCM 15801 (MCCC 1A00707).";
RL Submitted (JUN-2014) 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:KEK22691.1}.
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DR EMBL; JOTM01000027; KEK22691.1; -; Genomic_DNA.
DR RefSeq; WP_033677117.1; NZ_LTAQ01000056.1.
DR AlphaFoldDB; A0A073K810; -.
DR STRING; 574375.AZF08_14295; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000027778; 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 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 204..583
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 595 AA; 68850 MW; A7CF49235B100E08 CRC64;
MTELQNRLDV PDQEKWDLTD IYKSIEQWEH DYKKIETLTN ELKEFNGNIH DSKTLLAYLK
KSEEISGLFN LVYAYARLQS DLDTRDTEAQ SLVDKASQLH VKLSAARSFF SPFLLSIDEK
VLHSYIEENE ALQYYKEDLF ELYRYKKHVL NKDKEEILSQ MGEALSSPQH TYGMLNNADI
TFGEVTTDNG STVNLTRGMY SKLIKDENRN KRKEAYKAYY QPYIQLKNSI ASTLTGAIKN
NVTISKIRNY PSALEKSLFG DMVPKEVYDN LIDTTKKNIA SLHTYNHLRK EKLQLDELRQ
YDLNVNLVKG GNQDIPYDEA FEIMLTSLFP LSEEYLQTLK GFKDKRYIDV RELPGKRSGA
YNFGVYGVHP FILLNHNDDL NSLFTLTHEC GHGMHTYYSH GFQPRISAHY SIFVAEVAST
VNEILLIHHL LKEAKDTDVR KHLINHFIEQ FKGTFFTQVM FAEFEKITHE MAEQGKPLHA
QAFNDVYENL FREYNGDTLV FDEEVKYGWA RIPHFYRPFY VYKYATGFAS AIQIADQLLS
GDPIAQQNYI EFLKGGSSDY PLNLLKKTGV DLTTPTPIES ALGRFDKLVK EFSSL
//
