ID   K1ZM53_9BACT            Unreviewed;       514 AA.
AC   K1ZM53;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Insulinase family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACD_62C00629G0001 {ECO:0000313|EMBL:EKD50151.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD50151.1};
RN   [1] {ECO:0000313|EMBL:EKD50151.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD50151.1}.
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DR   EMBL; AMFJ01026432; EKD50151.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1ZM53; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 3.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..514
FT                   /note="Insulinase family protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017437998"
FT   DOMAIN          60..112
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          160..259
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          269..444
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   514 AA;  58372 MW;  A508E518347594B9 CRC64;
     MTKKICLYFL FPALFLGGFV TCSPHTPVPE TTKLAQSPAT DSFDLENRVK RIKLDNGLVV
     LLLRREGAPV FSVVNRVKVG NVEEVPGAYG LAHFFEHMAF KGTPTIGTDD FTREEPVLKE
     LYQVGTQIVR LQGEGDKPEE HASLTQKLDA LQKQDEALVN QNEFVNLLQR NGGANVNAAT
     GNDFTSYTVS LPSNKLELWA YMESERFLHP VMRDFFVEKK VVEEERRMRI DNTPQGLLVE
     KFLETAFVNH PYESLVIGPM KDIKAFVPAQ AREFFETYYI PSRMTLALVG NFELADAERI
     VRQYFGRLPA KADLGVKEAD AKFVPTGFPQ KVVLEKEDQP RFYLGYHRPA YRDPDDAVFD
     FVQQTLCAGR TSRLYQRLVL NEKKAVAVGC FSSFPGIRLN TLFAFYGTPV PGHTNDDLAK
     EIRIEVASLA AQGPTPEEMQ KINQTLDAEL IYDLQASSDL ASKLTFFESL MGDWHHLFEQ
     QKRYHQVTAE DVKRVTRKYF VAEREIMAAL EDRK
//