ID A0A1G1DZC4_9BACT Unreviewed; 498 AA.
AC A0A1G1DZC4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OGW12273.1};
GN ORFNames=A2W77_00625 {ECO:0000313|EMBL:OGW12273.1};
OS Nitrospinae bacterium RIFCSPLOWO2_12_39_16.
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota.
OX NCBI_TaxID=1801690 {ECO:0000313|EMBL:OGW12273.1, ECO:0000313|Proteomes:UP000178064};
RN [1] {ECO:0000313|EMBL:OGW12273.1, ECO:0000313|Proteomes:UP000178064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGW12273.1}.
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DR EMBL; MHDO01000045; OGW12273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1DZC4; -.
DR Proteomes; UP000178064; 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; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 47..88
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 149..242
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 253..427
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT COILED 119..146
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 498 AA; 57670 MW; 46ACE8B045E81471 CRC64;
MKRRKIFCLL SSVFFLIYLY IPASSETLDK RVVEHTLKNG MKLLLLERHQ SPIIATTIMF
KVGSVDERTG MTGIAHLLEH MLFKGTKMLG TKDYKKEKPL LDKMDKIAVQ LDTEERKGEK
IDKGKIEKLR SELKRLQDEH KNLIIKDEFA SLYSKQGGVG YNAGTSRDMT SYVISLPSNK
LELWAVIESD RMKNPVLREF YSERNVIMEE RRMSYDNDPE GSLFENFLSA AYNAHPYGMP
TIGWMSDIKF LPKKEVERFL KTYYAPNNCV VTVVGDIDAK KIIEMMDKYF VEIPPQNIPE
RVWTEEPEQI GERRIEVEFD ANPSIIIGYH KPTLPHHDDY VFDVIDFILG SGRTSRLYKK
MVEEKRIAVS VSTFSMPGSR YSNLFIFNGV PRAPHTVKEL EDAFYEEIER LKNEPVSAKE
LEKVINHLEA HHIRQLGSNR GMSDTLAYYQ TVAGNWKYMM THIDKIRKIT PEDVMNTAKK
YLIKNNRTVA VLVKKEGK
//
