ID   INA_BACTL               Reviewed;         687 AA.
AC   P23382;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Immune inhibitor A;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=ina;
OS   Bacillus thuringiensis subsp. alesti.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 47-87 AND
RP   200-242.
RC   STRAIN=BT75 / Serotype 3A;
RX   PubMed=2089225; DOI=10.1111/j.1365-2958.1990.tb00575.x;
RA   Loevgren A., Zhang M., Engstroem A., Dalhammar G., Landen R.;
RT   "Molecular characterization of immune inhibitor A, a secreted virulence
RT   protease from Bacillus thuringiensis.";
RL   Mol. Microbiol. 4:2137-2146(1990).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=BT75 / Serotype 3A;
RX   PubMed=6421577; DOI=10.1111/j.1432-1033.1984.tb08000.x;
RA   Dalhammar G., Steiner H.;
RT   "Characterization of inhibitor A, a protease from Bacillus thuringiensis
RT   which degrades attacins and cecropins, two classes of antibacterial
RT   proteins in insects.";
RL   Eur. J. Biochem. 139:247-252(1984).
CC   -!- FUNCTION: Neutral metalloprotease that is secreted to degrade
CC       antibacterial proteins produced by the insect host for its defense
CC       (attacins and cecropins). Probably degrades some unknown crucial
CC       protein(s) too, since it is toxic when injected to insect larvae.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M6 family. {ECO:0000305}.
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DR   EMBL; X55436; CAA39079.1; -; Genomic_DNA.
DR   PIR; S12399; S12399.
DR   AlphaFoldDB; P23382; -.
DR   SMR; P23382; -.
DR   MEROPS; M06.001; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR012300; Pept_M6_InhA.
DR   InterPro; IPR008757; Peptidase_M6-like_domain.
DR   Pfam; PF05547; Peptidase_M6; 1.
DR   PIRSF; PIRSF007519; Protease_InhA; 1.
DR   TIGRFAMs; TIGR03296; M6dom_TIGR03296; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..?25
FT                   /note="Or 32"
FT   PROPEP          ?26..40
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028642"
FT   CHAIN           41..687
FT                   /note="Immune inhibitor A"
FT                   /id="PRO_0000028643"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   687 AA;  75010 MW;  289E13E70CFBA91B CRC64;
     MKDAKADTKE KLNQPATGTP AATGPVKGGL NGKVPTSPAK QKAYNGDVRK DKVLVLLVEY
     ADFKHNNIDK EPGYMYSEDF NKEHYEKMLY GDEPFALEDG SKIETFKQYY EEQSGGSYTV
     DGTVTKWLTV PGKAADYGAD AATGHDNKGP KGPRDLVKDA LKAAVDSGLD LSQFDQFDQY
     DVNGDGNQNQ PDGLIDHLMI IHAGVGQEAG GGKLGDDAIW SHRWTVGPKP FAIEGTQAKV
     PYWGGKMAAF DYTIEPEDGA VGVNAHEYGH DLGLPDEYDT DYTGHGEPIQ AWSVMSGGTW
     AGKIAGTTPT SFSPQNKEFF QKTIGGNWAN IVEVDYEKLN KGIGLATYLD QSVTKSNRPG
     MIRVNLPDKD VKTIRPAFGK QYYYSTKGDN LHTTLETPLF DLTNATNAKF DFKSLYEIEA
     EYDFLEVHAV TEDGQKTLIE RLGEKANSGN AEATNGKWID KSYDLSQFKG KKVKLTFEYI
     TDGGLALNGG LLDNASLTVD GKVTFSDDAE GTPQLKLDGF VVSSGTEKKK HNYYVEWRNH
     TGSDSALKFA RGPEYNSGMV VWYADSAYAD NWVGLHPGHG FLGVVDSHPE AIVGTLNGKP
     TIDSSTRFQI ADAAFSFDKT PAWKVVSPTR GTYTYDGLAG VAKFDDSKTY INQQIPDAGR
     ILPKLGLKFE VVGQADDNSA GAVRLYR