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Database: UniProt
Entry: A0A154BTI8_ANASB
LinkDB: A0A154BTI8_ANASB
Original site: A0A154BTI8_ANASB 
ID   A0A154BTI8_ANASB        Unreviewed;       415 AA.
AC   A0A154BTI8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:KYZ77242.1};
GN   ORFNames=AXX12_03675 {ECO:0000313|EMBL:KYZ77242.1};
OS   Anaerosporomusa subterranea.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Anaerosporomusa.
OX   NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ77242.1, ECO:0000313|Proteomes:UP000076268};
RN   [1] {ECO:0000313|EMBL:KYZ77242.1, ECO:0000313|Proteomes:UP000076268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU4 {ECO:0000313|EMBL:KYZ77242.1,
RC   ECO:0000313|Proteomes:UP000076268};
RA   Choi J.K., Shah M., Yee N.;
RT   "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming obligate
RT   anaerobe isolated from saprolite.";
RL   Submitted (FEB-2016) 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}.
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:KYZ77242.1}.
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DR   EMBL; LSGP01000013; KYZ77242.1; -; Genomic_DNA.
DR   RefSeq; WP_066239222.1; NZ_LSGP01000013.1.
DR   AlphaFoldDB; A0A154BTI8; -.
DR   STRING; 1794912.AXX12_03675; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000076268; 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:UniProtKB-KW.
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;
KW   Hydrolase {ECO:0000313|EMBL:KYZ77242.1};
KW   Protease {ECO:0000313|EMBL:KYZ77242.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076268}.
FT   DOMAIN          12..158
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   415 AA;  46449 MW;  200129DC23359BAB CRC64;
     MYEKSVLNNG IRVVTETMPH LRSVTLGAWV ATGSRYEQPN NHGISHFIEH LLFKGTTTRS
     AKAIAEEVDS VGGQLNAFTG KEYTCYYMKS LDTHLDLAIE LISDMLLNAR FDPNDIAKEK
     GVVLEEYNMY EDSPDELVHD LYVQQVWQDH PLGQSILGSR QSIERFNRQM ILDYRQSHYT
     PDNIVIAAAG NLTHAQVLTL AERYFGKMSG AAGGQTALAP RYLPIQSSRT KDTEQAHICL
     GAPGFKYDAD ELYSLHILNN LLGGSMSSRL FQSIREDRGL AYSVYSYQSS YKDTGLLTIY
     AGTRPDNVNE VLDLIWRNMT DLRKNGVSET ELHKAKEQLK GNLFLGLESS SSRMSRIGTL
     EMTVGKYVTL DEVIAKIDRV SAVDIASVAS ALFQPEMISC YILGPEQDIK FGKFI
//
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