ID A0A0R2PET4_9ACTN Unreviewed; 425 AA.
AC A0A0R2PET4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:KRO36398.1};
GN ORFNames=ABR54_05680 {ECO:0000313|EMBL:KRO36398.1};
OS Actinobacteria bacterium BACL15 MAG-120619-bin91.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetes incertae sedis;
OC ac1 cluster.
OX NCBI_TaxID=1655562 {ECO:0000313|EMBL:KRO36398.1, ECO:0000313|Proteomes:UP000053274};
RN [1] {ECO:0000313|EMBL:KRO36398.1, ECO:0000313|Proteomes:UP000053274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL15 MAG-120619-bin91 {ECO:0000313|EMBL:KRO36398.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:KRO36398.1}.
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DR EMBL; LIAM01000011; KRO36398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2PET4; -.
DR Proteomes; UP000053274; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KRO36398.1};
KW Protease {ECO:0000313|EMBL:KRO36398.1}.
FT DOMAIN 13..160
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..345
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 425 AA; 46567 MW; F4867E8F8D859E5F CRC64;
MSVRRSVLPS GLRIVTEEVP SVRSAAIGIW VNVGSRDETP AVAGASHFLE HLLFKGTKRR
NALEISSSIE SVGGEMNAFT SKEYTCFYAR VIDTDLPMAI DVVSDLITSS VVTALDVDAE
RKVVLEEIAM RDDDPSDLVH DLYAETYYGD TPLGRPILGT IDSINNMSRN SVFNYYKKRY
LPQDLVVAVA GNIRHKKVVA MVEAALSQDG FLDVTGAPVI RPNTLIRKSL QRSVGLISRP
TEQAHMFYGM EGVARHDDRR FAMGILASAL GGGMSSRLFQ EIREKRGLAY SVYAYAQQFA
GSGQIGFYAG CNPAKAIEVV EIIREVLADV ADNGMSHEEI ERAKGAVRGS LVLSQEDSGS
RMSRIGKNEI VYGHVMDFDE ILKAISRVND TDIKEIASAF LSKTPTLALV GPFKSESKFE
KVLSK
//