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Database: UniProt
Entry: E7NAN4_9ACTO
LinkDB: E7NAN4_9ACTO
Original site: E7NAN4_9ACTO 
ID   E7NAN4_9ACTO            Unreviewed;       263 AA.
AC   E7NAN4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Peptidase, M16 family {ECO:0000313|EMBL:EFW26760.1};
DE            EC=3.4.24.- {ECO:0000313|EMBL:EFW26760.1};
DE   Flags: Fragment;
GN   ORFNames=HMPREF9057_01854 {ECO:0000313|EMBL:EFW26760.1};
OS   Actinomyces sp. oral taxon 171 str. F0337.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=706439 {ECO:0000313|EMBL:EFW26760.1, ECO:0000313|Proteomes:UP000005722};
RN   [1] {ECO:0000313|EMBL:EFW26760.1, ECO:0000313|Proteomes:UP000005722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0337 {ECO:0000313|EMBL:EFW26760.1,
RC   ECO:0000313|Proteomes:UP000005722};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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:EFW26760.1}.
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DR   EMBL; AECW01000288; EFW26760.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7NAN4; -.
DR   MEROPS; M16.A15; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_4_1_11; -.
DR   Proteomes; UP000005722; 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; 1.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 1.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EFW26760.1}.
FT   DOMAIN          64..212
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         263
FT                   /evidence="ECO:0000313|EMBL:EFW26760.1"
SQ   SEQUENCE   263 AA;  27579 MW;  C4203E9648DD9A1A CRC64;
     MRPGSARPAA SQPSSTPATG ESSSPTDYAE VDLGRGRPGR DGTELTLHDD GALTRRSVLP
     GGVRVITESV PGLRSASIGM WFGVGSRDEV PGQEGSTHFL EHLLFKGTAT RDAHDIAEAF
     DMIGGESNAA TSKEHTSYYA RVLAPDSMQA LDVLADMVTS SLLEPTDVET ERGVIVSELA
     DAADDPADVA QEAFARAAFG EDTPLGRPIG GTNETVTAVP RDAVWEHYRR TYASDTLVVA
     AAGAVDHDEG CERGLADLAA AGW
//
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