ID A0A1M5VN13_9BACI Unreviewed; 602 AA.
AC A0A1M5VN13;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=SAMN05421807_11311 {ECO:0000313|EMBL:SHH76617.1};
OS Virgibacillus chiguensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=411959 {ECO:0000313|EMBL:SHH76617.1, ECO:0000313|Proteomes:UP000184079};
RN [1] {ECO:0000313|EMBL:SHH76617.1, ECO:0000313|Proteomes:UP000184079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6496 {ECO:0000313|EMBL:SHH76617.1,
RC ECO:0000313|Proteomes:UP000184079};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQXD01000013; SHH76617.1; -; Genomic_DNA.
DR RefSeq; WP_073010774.1; NZ_FQXD01000013.1.
DR AlphaFoldDB; A0A1M5VN13; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000184079; 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 118..187
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 208..587
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 602 AA; 69443 MW; 1AD70ADA38AF9103 CRC64;
MAKANKELPK RTELPVELTW RLEDIFETDE AWGQELADLQ KAIPEIENYQ GVLGSSAKNL
YEVLKLQDQL SERLGKLFTY AHMRYDQDTT NSFYQRINAQ AENVITVASS KMSYIVPEIL
EINEATLKQF LQEEEGLQGY QKTLDEITRQ RPHILNKREE AILAEASEPL GTASQTFGML
NNADLTFPSI KDEDGEEVDV THGRYIRFME SQDRSVRKAA FQAMYETYGA FKNTFASTLS
GNIKKDNFVA KVRNYESARQ AALDNNHIPE KVYDNLVEAV NERLPLLHRY IQLRKKVLEL
DELHMYDIYT PLVRDVDMEI TYEKAQQYVL EGLAPLGEGY LNIVKEAYNN RWIDVEENKG
KRSGAYSSGA YGTNPYILLN WQDNVNDMFT LAHELGHSVH SYYTRNNQPY RYGNYSIFVA
EVASTCNEAL LNDYLLKNLT DEKQKLYVLN HFLEGFRGTV FRQTMFAEFE HMIHVKQQQG
EALTAEKLTE LYYDLNKKYY GDDVVSDEEI GLEWARIPHF YYNYYVYQYA TGYSAATALA
QQILTEGDGA VERYTNFLKA GSSEYPIEVL QKAGVDMNSK QTILDALDVF AEKLEQLEDL
LK
//
