ID   A0A1Q7QHN2_9CHLR        Unreviewed;       429 AA.
AC   A0A1Q7QHN2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AUI58_08395 {ECO:0000313|EMBL:OLD51241.1};
OS   Chloroflexi bacterium 13_1_40CM_2_70_6.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1805070 {ECO:0000313|EMBL:OLD51241.1, ECO:0000313|Proteomes:UP000185765};
RN   [1] {ECO:0000313|EMBL:OLD51241.1, ECO:0000313|Proteomes:UP000185765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(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}.
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:OLD51241.1}.
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DR   EMBL; MNHK01000110; OLD51241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7QHN2; -.
DR   Proteomes; UP000185765; 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: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          13..158
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          168..339
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   429 AA;  47128 MW;  4F646A579C90CF36 CRC64;
     MEHRRVTMAN GLRVLVAEMP ETRSVSIAVY VGVGSRVESK LDAGTSHFLE HMVFKGTAKR
     PTAADISQEI ESRGGLVNAS TDKEVTVFWS RVPARHYLVA LDVIADMIRA PMLRPDDVES
     ERRVVVEELR MYRDQPQDRV HTLIDELLYP RHPLGWEVAG REQVVLAMDA DALRAFMSRN
     YAPGRSVVAL AGRLVADEAI AAVQEQFAFL GAREAPAFVP APQAGKVRAK VVGKRAEQTH
     LCIGWRTVPT DHPDKFTVDM LNAVLGEGMS SRLFLELREK RGLAYDVHSY DSNYADAGHL
     VVYAGFAPAK TAEVTTAVLR EVARLRDEGV PDAELERVRD FAKGRMELRL EDTRGVSSWL
     AGQELFLGRV RTVEEVCAII DGIGPDDIQR AARTYLRPEL AYVAAVGPRA SIAAVAPPAA
     EPVAMGIAS
//