ID   A0A1Y2QZY6_9BURK        Unreviewed;       467 AA.
AC   A0A1Y2QZY6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OSZ73453.1};
GN   ORFNames=CAP37_17680 {ECO:0000313|EMBL:OSZ73453.1};
OS   Hydrogenophaga sp. IBVHS1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1985169 {ECO:0000313|EMBL:OSZ73453.1, ECO:0000313|Proteomes:UP000194358};
RN   [1] {ECO:0000313|EMBL:OSZ73453.1, ECO:0000313|Proteomes:UP000194358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBVHS1 {ECO:0000313|EMBL:OSZ73453.1,
RC   ECO:0000313|Proteomes:UP000194358};
RA   Orr R.J.;
RT   "Draft genome sequences of novel bacteria, isolated from environmental
RT   samples.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OSZ73453.1}.
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DR   EMBL; NFUU01000002; OSZ73453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2QZY6; -.
DR   STRING; 1985169.CAP37_17680; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000194358; 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: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; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000194358};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..467
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013299702"
FT   DOMAIN          59..197
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          206..394
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   467 AA;  50950 MW;  15D02125AC7BEFE3 CRC64;
     MKRSPRLLFA RLGACFSPLV LVLALTLPGG AGAQAPPASA ARSFTLANGM TLIVRPDRRA
     PTVVHMLWVR VGSMDEVDGT SGVAHVLEHM MFKGTPDLAP GEFSRRVAAL GGRENAFTSR
     DATAYHQQVP AERLEDVMKL EADRFARNQW DDAEFKREIE VIKEERRQRT EESPRSRMYE
     ALNAMVYQAS PYRRPIIGWM SDLDAMTPDD ARNFYRQWYS PSNAAVVVAG DVDVDQVLAL
     AQKHYGAIPA RVVPARKPRE EPPQLGPRRM EYRAVAEQAV VALVYKAPRW VGDDSSKSQD
     ALALTVLAAV LDGYSGARLD RALVQGAGHG GKRFADGASA SFGLMGRGPQ EFSLSAVPAR
     GVSAEMAAAA LKTEVARIAR EGVSDAELRR VKTQWTASEV YKLDSVVNQA RELGSYWING
     MGLDAGERLM AQLRGVSAAQ VQSVAQRYFS DDQLTTAVLV PTPPAAK
//