ID A0A0M4FVP8_9BACI Unreviewed; 597 AA.
AC A0A0M4FVP8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Oligoendopeptidase {ECO:0000313|EMBL:ALC89861.1};
GN ORFNames=AM500_08805 {ECO:0000313|EMBL:ALC89861.1};
OS Bacillus sp. FJAT-18017.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC89861.1, ECO:0000313|Proteomes:UP000060713};
RN [1] {ECO:0000313|EMBL:ALC89861.1, ECO:0000313|Proteomes:UP000060713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC89861.1,
RC ECO:0000313|Proteomes:UP000060713};
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 (AUG-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}.
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DR EMBL; CP012602; ALC89861.1; -; Genomic_DNA.
DR RefSeq; WP_053598875.1; NZ_CP012602.1.
DR AlphaFoldDB; A0A0M4FVP8; -.
DR STRING; 1705566.AM500_08805; -.
DR PATRIC; fig|1705566.3.peg.1893; -.
DR Proteomes; UP000060713; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09607; 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 InterPro; IPR034006; M3B_PepF_2.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 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|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000060713};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 120..183
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 205..583
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 597 AA; 67421 MW; 8DBA775BABF9EA03 CRC64;
MSVNTYSDVW DLDVFFPGGS ASKEFEAHLT DTEGTINQFY SKVKSWQPSI VEKDADLLAV
LISLFEEASK KIRQAGAFIS CLKAQNTEDK KAYELQSKVT GLSASFQTAL GALDGSLTGI
AEEAWQKLME DDRLNELAFV LTERRTRAAE KLSKEEEAVV NALGVDGYHA WGQMYDMVVG
KMKIPFTQNG EEKLLSVGQA ANQFSNPDRE VRKAVFKEWE TAWSANADYF AKILNHLAGF
RLSVYKLRGW DDFLKEPLDI NRMSKETLDA MWGAISEAKQ PLKKYLERRA ELMGVEKLSW
FDLDAPYGNT ETKVSYQEGA EFILEQFAKF GEEMTSFSRH AFENNWIEAE DRPGKAPGGF
HTYFPEAMQS RIFMTYSGTP SNISTLAHEL GHGFHTYAMR NLHLLNRNYA MNVAETASTF
AEMIVSDAAV KNASSKDEKL ALLDDKIQRS VALLMNIHAR YLFETSFYEE RKAGFVSAAR
LNGLMEKAQE EAYLGALDSY HPSFWASKLH FFITGVPFYN FPYTFGFLFS LGIYAQALEE
GSGFEEKYVA LLKDTASMTV EELAMKHLGA DLTKADFWKD ALQLCTDDIN EFLELTK
//
