ID A0A0S1SVW4_9BACT Unreviewed; 419 AA.
AC A0A0S1SVW4; A0A0S1SIG9; A0A0S1SM45; A0A0S1SMB5; A0A0S1SQQ2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Zn-dependent peptidase {ECO:0000313|EMBL:ALM13586.1};
GN ORFNames=PeribacterD1_0919 {ECO:0000313|EMBL:ALM13586.1};
OS Candidatus Peribacter riflensis.
OC Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria;
OC Candidatus Peribacterales; Candidatus Peribacteraceae; Peribacter.
OX NCBI_TaxID=1735162 {ECO:0000313|EMBL:ALM13586.1, ECO:0000313|Proteomes:UP000069135};
RN [1] {ECO:0000313|Proteomes:UP000069135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA Thomas B.C., Williams K.H., Banfield J.F.;
RT "Analysis of five complete genome sequences for members of the class
RT Peribacteria in the recently recognized Peregrinibacteria bacterial
RT phylum.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALM13586.1, ECO:0000313|Proteomes:UP000069135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIFOXYD1_FULL_PER-ii_59_16 {ECO:0000313|EMBL:ALM13586.1};
RX PubMed=26844018;
RA Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA Thomas B.C., Williams K.H., Banfield J.F.;
RT "Analysis of five complete genome sequences for members of the class
RT Peribacteria in the recently recognized Peregrinibacteria bacterial
RT phylum.";
RL PeerJ 4:E1607-E1607(2016).
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}.
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DR EMBL; CP013065; ALM13586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S1SVW4; -.
DR STRING; 1735162.PeribacterB2_0921; -.
DR KEGG; prf:PeribacterA2_0919; -.
DR PATRIC; fig|1735161.3.peg.897; -.
DR Proteomes; UP000069135; Chromosome.
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:InterPro.
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;
FT DOMAIN 19..135
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 169..340
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 419 AA; 46843 MW; FABACCA6EE0749AB CRC64;
MYSIQRLASG LPVLTAPSDG VESATVMVFA GAGSRYERQQ NRGISHFLEH MFFKGGDKYL
TTKDVSAAIE GVGGDFNAFT GKEYAGYYVK AAAKHLDLSC DVLSDMLCNA KFPQEEIEKE
RGVIMEEERM YQDTPMYRAG WDFEQLLYGD HPLGWDTIGT EKVIQSVQTS DFLHHKEELY
TPDNLVLAFA GKVDQAQALA LAERYFRPIG GKKSHAFDPF TTFGSDRVYL RTKKTEQAHL
VLGVPGVGAL DGDHFAHKLL SIILGGNMSS RMFLNIREAK GLCYYIATEV DSYLDGGSLS
TRAGIDQTRL HEAITLIIHE YDQCAASGVT AEELTRAKDY LTGRVTLSLE DTEERAHFYG
KQQLLYPKVR DLPQYFAEIA KVTQEQVNAL AKRLLTHKDL RLVVIGQEEN KAKLEELIV
//
