ID   E8WMY8_GEOS8            Unreviewed;       418 AA.
AC   E8WMY8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:ADW12643.1};
GN   OrderedLocusNames=GM18_1169 {ECO:0000313|EMBL:ADW12643.1};
OS   Geobacter sp. (strain M18).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW12643.1, ECO:0000313|Proteomes:UP000001442};
RN   [1] {ECO:0000313|EMBL:ADW12643.1, ECO:0000313|Proteomes:UP000001442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18 {ECO:0000313|EMBL:ADW12643.1,
RC   ECO:0000313|Proteomes:UP000001442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA   Aklujkar M., Lovley D., Woyke T.;
RT   "Complete sequence of Geobacter sp. M18.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP002479; ADW12643.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8WMY8; -.
DR   STRING; 443143.GM18_1169; -.
DR   KEGG; geb:GM18_1169; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_3_7; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000001442; Chromosome.
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          12..159
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          166..339
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   418 AA;  46813 MW;  0D59D99EF1CE2C60 CRC64;
     MIKKTTLNSG IRVITERIPY ASSVSIGIWV ANGSRHERRE SNGVAHFIEH LLFKGTDRRS
     SLDIAREIDS VGGVLNAFTS REYVCYYAKV LDKFLPRAVD LLTDIFLHST FDNEEIEKER
     RVVLQEINMM EDTPDDLIHD LFHQHFWKGH PLGMSILGDA ESVTGLSRDA IIAYKDQMYR
     ADDIIVTAAG NVAHDKLTAL LEEFLHGVEP GHGRCESAPP VYERRIELVE KDLEQIHVCL
     GLKGVQQSHP QRYDAFIMNA ILGGSMSSRL FQEVREKSGL AYSVYSYIAS HADAGSLVVY
     AGASPENSKE LLEIMLREIG RFKTEPVPAD QLEGAREQLK GNLLLSLESS DNRMSRLAKN
     EIYFGTPLPL TDIMEGFDRV TSESIQQLAR EILDNSALTL VMLGRIGTPF FTASDINV
//