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Database: UniProt
Entry: A0A1W9VRE5_9BACT
LinkDB: A0A1W9VRE5_9BACT
Original site: A0A1W9VRE5_9BACT 
ID   A0A1W9VRE5_9BACT        Unreviewed;       850 AA.
AC   A0A1W9VRE5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B6226_02940 {ECO:0000313|EMBL:OQY38868.1};
OS   Candidatus Cloacimonetes bacterium 4572_65.
OC   Bacteria; Candidatus Cloacimonadota.
OX   NCBI_TaxID=1972455 {ECO:0000313|EMBL:OQY38868.1, ECO:0000313|Proteomes:UP000231707};
RN   [1] {ECO:0000313|EMBL:OQY38868.1, ECO:0000313|Proteomes:UP000231707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4572_65 {ECO:0000313|EMBL:OQY38868.1};
RX   PubMed=28835260; DOI=.1186/s40168-017-0322-2;
RA   Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.;
RT   "Genomic insights into potential interdependencies in microbial hydrocarbon
RT   and nutrient cycling in hydrothermal sediments.";
RL   Microbiome 5:106-106(2017).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:OQY38868.1}.
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DR   EMBL; NBMD01000045; OQY38868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9VRE5; -.
DR   Proteomes; UP000231707; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
FT   DOMAIN          15..144
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          170..344
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          609..783
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   850 AA;  97756 MW;  B3AC17F6DDE8D996 CRC64;
     MKANLKHYDL DNGFRVILAK DSSNPILSVQ LFIKVGSVHE PAEESGFSHL TEHLVFKSTE
     NYPTNGIMER ASFLGANINA YTEFESTCLY LTLPSKFGED ALDILSQLVY KSNYSDEEFF
     TERNVVIEEL KQYENDPEDN FLEKAPLLCF TESPYHNLII GNLANIENST PQQLRDFYKK
     YYIPQNCYLV ITGDFEETEI KAQIDKYFGE WQSAELNKLE NRKNDYIQDF RVIHVEEKDI
     VQDMLAFVVP EINESSLKGL ALSIITKGFA IGRNSRLHKR LYLKEQLVSG IQVHSIAGTY
     EGISEILIVP KNNSNLEKIS RIFLEEIALL CASGFTADEL RKLKVEQENG WKYSFEYMEN
     FASVLGNEEL DLGYKEFMNF PTRLAAVDSK LIRDVLHEYY SLDKLKILHL GTKNEKLLAL
     EEEIKNRVEV EDICIIPKVE KITGDYHEHL CENGMKLLIK KVVGKPTVGI SLARRFSQLN
     ESLNRRGLTY FMTALMQYGN EKYSYEELLD YCNEKGINFH ISNGIETAGV KAKCFVDQVS
     ASIKLMADVI KTPLLPTREL LNLKDSVKSD LRRYPDFPMK DANKKYNQFI LGKRSNLILK
     TGELSDIVKI SRKEIVEWHK EFLDLSKMTI AVVGDVDFVD VIREVENSFN FDFTKSKSVQ
     KAAYIKGARK RTIYKNGNDQ SIIHIGGFAC NSTNRRHNTA FHVLSQIIGG DMNSRLFNEL
     REKQGVAYSV DFDYSSLEDI GVFNNFAVVD RAREEQAIKT IYAIMQDIKD NNVTPEELQL
     TKNFINGQRL IDNESVIAQA DQLSLLSALG YSYDYYLQRE NRLNNVSHED IDEIANSYFN
     RKDLYMQIYR
//
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