ID A0A1L4C1J9_9LACT Unreviewed; 602 AA.
AC A0A1L4C1J9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Oligoendopeptidase {ECO:0000313|EMBL:API89969.1};
GN ORFNames=BKP56_12180 {ECO:0000313|EMBL:API89969.1};
OS Marinilactibacillus sp. 15R.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Marinilactibacillus.
OX NCBI_TaxID=1911586 {ECO:0000313|EMBL:API89969.1, ECO:0000313|Proteomes:UP000184433};
RN [1] {ECO:0000313|EMBL:API89969.1, ECO:0000313|Proteomes:UP000184433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15R {ECO:0000313|EMBL:API89969.1,
RC ECO:0000313|Proteomes:UP000184433};
RA Wei Y., Cao J., Fang J.;
RT "Genome sequence of Marinilactibacillus sp. 15R.";
RL Submitted (OCT-2016) 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; CP017761; API89969.1; -; Genomic_DNA.
DR RefSeq; WP_072695447.1; NZ_CP017761.1.
DR AlphaFoldDB; A0A1L4C1J9; -.
DR STRING; 1911586.BKP56_12180; -.
DR KEGG; marr:BKP56_12180; -.
DR Proteomes; UP000184433; 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:UP000184433};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 117..178
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 202..584
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 602 AA; 68514 MW; 90FF988A29CDFEC8 CRC64;
MSYQLNWDMD SVFTGGSQSS ELRTKIETLK EQIEQFHQTV ELWDPEVDRL NYNHLKEVLN
LSEKIGNSLS EAMTFSRGLL SANVRDKNAA KLTNELSTLY SSLSNSTTVL TKKYVGIDDA
DWADLLEIEP FNASAFPLNE QREQGKKLLS QNEEAVINAL TNDGFKGWGD LYNSLVATVQ
VDFENKDGKV NSYSAGQAAN LMGSAKDPET RQKMLEKWEL AWASKSSLFA DTLNHLAGFR
LENYKLHGTE DFMARPLEYN RLKKETLDIM WDTITKNKPK VVEYLNRKAQ LMGIEKLSWV
DVTAPVSVGD FEPRHYSYDE AAEFIMENFS SFSNQMQKLA KTAFEDSWIE AEYRDGKRPG
GYCANLPESE QSRIFMTFSG SAGNVSTLAH ELGHAFHSYV MRDLPVMNRR YAMNVAETAS
TFAELVISDA TVREASSEAE KINLLDSKNA RAATMFMNIH SRYLFETAFY EERKNGIVTD
DRLSELMVDA QKEAYQDSLS TYHPTFWASK LHFYNTGVPF YNFPYTFGFL FSLGIYARSL
EEGSGFEEKY IALLRDTASM TTEALAQKHL NVDLTQPDFW QSAIDMVHAD IDEYLELTAK
YI
//
