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Database: UniProt
Entry: A0A4S8HXC1_9BACT
LinkDB: A0A4S8HXC1_9BACT
Original site: A0A4S8HXC1_9BACT 
ID   A0A4S8HXC1_9BACT        Unreviewed;       953 AA.
AC   A0A4S8HXC1;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Insulinase family protein {ECO:0000313|EMBL:THU39931.1};
GN   ORFNames=FAM09_08540 {ECO:0000313|EMBL:THU39931.1};
OS   Niastella caeni.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=2569763 {ECO:0000313|EMBL:THU39931.1, ECO:0000313|Proteomes:UP000306918};
RN   [1] {ECO:0000313|EMBL:THU39931.1, ECO:0000313|Proteomes:UP000306918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HX-2-15 {ECO:0000313|EMBL:THU39931.1,
RC   ECO:0000313|Proteomes:UP000306918};
RA   Sheng M.;
RT   "Niastella caeni sp. nov., isolated from activated sludge.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:THU39931.1}.
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DR   EMBL; STFF01000002; THU39931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S8HXC1; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000306918; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
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          55..173
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          214..393
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          694..872
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   953 AA;  106574 MW;  B28D03A7DC9ACE4A CRC64;
     MMYSLRVGTR WLLLLVGILS IEYATAQLNM ESKLPVDAKV KIGKLENGLT YYIRQNKKPE
     QKVELRLVLN AGSILEDDDQ QGLAHMAEHM AFNGTTHFKK NDIVSFLQDI GVGFGNDLNA
     YTGFDETVYI LPIPTDKPGN LDKGFQVLED WAHNVTYLDD DINGERAIIL EESRLGKGAN
     ERIFRKIYPQ LFEGSKYAKR LPIGVDSIIK NFPVNNIRRY YKDWYRPDLM AVVVVGDIEL
     AKAEAMVKKH FSRLTNPANA RKREYADVPP YTSSQAMVVT DKEATGYQVA INYPAIKKSP
     AVTIGDYRKD LIEQMYVSML NERLQELTQK ENPPFIYGAA DFDSYARGYQ SFNAMAAAGT
     GDIQKALNAL AEEIERVKRF GFTADELQRA KKTMLAHYET AFNNRGKTES ADYVEEYMNN
     FLVQEPIPGI EKEFEYAKAL LPAIKLDEVN AVSNAFKDQK NLFVYMSGPE SMDTTALPSE
     KDLLAIIDAR AKADIKPYEE KAVATTLLSK EPKAGKVIAV TKYPLLGTTD YKLSNGVTVT
     LKPTDFKNDQ IIMGATRPGG KNSYGLADKY NAEYMTAVTG AMGVGGFSPT DLSKALAGKT
     VNVAPVFTTI SDGFHGTSSV KDLETMFQLT YLQCTAPRGD TALFRAFVQR NKLQFAKISA
     NPQAAFVDTL YKTLFGNNPL AQVIVPNSAY FDMISYDRVL AIHKERYGDV SGMHFVFAGS
     FKESEIKPLI EKYIASLPAT GKKFTIVDNK VRPISGKKTF VVNKGKEDKS LILAFYSGET
     PYNEDMELKA QALSEVLNIR IIEELREKIQ GIYGGGTSAD VGKYPYPNYN FVVQLPCGPE
     KVDTLVKAIK KEFSDMVAKG PDTTYLNKVK KQWLEQHKLN VKDNGFWVER LLQYKLQGGN
     PDRFVHYEKY VKMLTPKDVQ QAAKLMFDGN EFVAIQMPEN AKGGTGAESK KGF
//
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