ID A0A1J5H282_9BACT Unreviewed; 421 AA.
AC A0A1J5H282;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUK07_00585 {ECO:0000313|EMBL:OIP75898.1};
OS Parcubacteria group bacterium CG2_30_36_21.
OC Bacteria.
OX NCBI_TaxID=1805315 {ECO:0000313|EMBL:OIP75898.1, ECO:0000313|Proteomes:UP000183564};
RN [1] {ECO:0000313|EMBL:OIP75898.1, ECO:0000313|Proteomes:UP000183564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_36_21 {ECO:0000313|EMBL:OIP75898.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIP75898.1}.
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DR EMBL; MNZD01000009; OIP75898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5H282; -.
DR STRING; 1805315.AUK07_00585; -.
DR Proteomes; UP000183564; 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 14..135
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..340
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 421 AA; 48376 MW; 1F190F22312A80CE CRC64;
MYKKTTLKNG LRIITVPMKS TRAVTVLVVV GTGSKYETKE INGISHFLEH MFFKGTKNRP
TTLKIAETLD KVGGVYNAFT SEEFTGYWAK VGWRHLDLAL DWVSDIFLNS KLEQKEIKRE
KGVIIEEINM YLDTPVGYIG DLWEKLLYGD QPAGWLTIGE KKNILKFERG HLLDYFRNHY
STLNTVVCIA GNFNQKEVKK KIKRYFKNLK KKPPKEKLKV IEKQKRPQSL VYYKKTDQTH
LCLGVRGYNL FHSEKYAQEI LATILGANMS SRLFISVRAK KGLCYYIRTS SDYSTDTGYL
VTQAGVPHKN IGKVIDLILK EYKNLKTKKV SAQELQKAKD YLKGVSILSL ESSDVRASFY
SLQELLSRKI LTPEEKFAKL DKVTPNDVQK AARNIFRPEK LNLALIGPHK DNSKFQQLLK
L
//
