ID A0A0M9GS60_9BACI Unreviewed; 603 AA.
AC A0A0M9GS60;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=AAV98_13280 {ECO:0000313|EMBL:KPB04219.1};
OS Bacillus sp. CHD6a.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1643452 {ECO:0000313|EMBL:KPB04219.1, ECO:0000313|Proteomes:UP000037908};
RN [1] {ECO:0000313|EMBL:KPB04219.1, ECO:0000313|Proteomes:UP000037908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHD6a {ECO:0000313|EMBL:KPB04219.1,
RC ECO:0000313|Proteomes:UP000037908};
RA Lin W., Liu Y., Zheng Q., Jiao N.;
RT "Genome sequence of Bacillus sp. CHD6a isolated from the shallow-sea
RT hydrothermal environment.";
RL Submitted (APR-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:KPB04219.1}.
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DR EMBL; LBMD01000016; KPB04219.1; -; Genomic_DNA.
DR RefSeq; WP_060666053.1; NZ_LBMD01000016.1.
DR AlphaFoldDB; A0A0M9GS60; -.
DR PATRIC; fig|1643452.3.peg.1518; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000037908; 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; cd09609; 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; IPR034009; M3B_PepF_4.
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; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 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 211..588
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 603 AA; 68519 MW; 982E41429089FB03 CRC64;
MAKVMDKALK REEVPVEQTW NLKDLFVSSE AWEQELQAVQ QDLSTVTYYK GKVGKDAKSL
LGCLKDKDAL TERVMRVMTF ASLKQSEDGT NPENQANSTR VGGMISNFSA STSFIQSEIL
QLNEETLNAF TAEEPELEEF KKSLMDVMET KPHKLSPEAE EVLSAFGEVH NAPYTIYQRS
LISDMRFPSF FTDDGQEHPL SFNSFPNYEG SSNTELRRKA YQTYIDTLKQ YKHTYAATYA
TEVKKQVVEA RLRNYESVTD MLLFDQQVTK EMYHNQLDII QSELAPHMQR YAKLKKRVLG
LETMQFCDLK APLDPDFNPE ITYEEASELI LESLKVMGPE YMEIMKEGLN NRWVDLADNV
GKGSGAFCSS PYGVHPYILM TWSDSMRNAF TLTHELGHAG HFRLAGRYQK LSNTRPSRYF
VEAPSTMNEM LLSQHILSKP NDERMRRWVI LQSLGTYYHN FVTHILEGEL QRRVYDLADK
GTPITANVLC DQKTALLSEF WGDAVEMDEG AGLTWMRQPH YYMGLYPYTY SAGLTASTAA
AKQIQKEGQP AVDRWLSALK AGGTLKPLEL MQLGGVDMTT SEPIKTAVAY VGSLIDELEK
SFS
//
