ID   MARI_ALTSP              Reviewed;          63 AA.
AC   P29399; Q9WWQ5;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 3.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Marinostatin-L;
DE   Contains:
DE     RecName: Full=Marinostatin-C1;
DE   Contains:
DE     RecName: Full=Marinostatin-C2;
DE   Contains:
DE     RecName: Full=Marinostatin-D;
DE   Flags: Precursor;
GN   Name=mstI;
OS   Alteromonas sp. (strain B-10-31).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=29456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-60.
RX   PubMed=9972273; DOI=10.1271/bbb.62.2446;
RA   Miyamoto K., Tsujibo H., Hikita Y., Tanaka K., Miyamoto S., Hishimoto M.,
RA   Imada C., Kamei K., Hara S., Inamori Y.;
RT   "Cloning and nucleotide sequence of the gene encoding a serine proteinase
RT   inhibitor named marinostatin from a marine bacterium, Alteromonas sp.
RT   strain B-10-31.";
RL   Biosci. Biotechnol. Biochem. 62:2446-2449(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 43-56, PYROGLUTAMATE FORMATION AT GLN-43, AND REACTIVE
RP   SITE.
RX   PubMed=1794974; DOI=10.1093/oxfordjournals.jbchem.a123678;
RA   Takano R., Imada C., Kamei K., Hara S.;
RT   "The reactive site of marinostatin, a proteinase inhibitor from marine
RT   Alteromonas sp. B-10-31.";
RL   J. Biochem. 110:856-858(1991).
RN   [3]
RP   STRUCTURE BY NMR OF 45-56.
RX   PubMed=15709758; DOI=10.1021/bi048034x;
RA   Kanaori K., Kamei K., Taniguchi M., Koyama T., Yasui T., Takano R.,
RA   Imada C., Tajima K., Hara S.;
RT   "Solution structure of marinostatin, a natural ester-linked protein
RT   protease inhibitor.";
RL   Biochemistry 44:2462-2468(2005).
CC   -!- FUNCTION: Inhibits subtilisin, chymotrypsin, and elastase, but not
CC       trypsin.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I10 family.
CC       {ECO:0000305}.
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DR   EMBL; AB011418; BAA81783.1; -; Genomic_DNA.
DR   PIR; JE0393; JE0393.
DR   PDB; 1IXU; NMR; -; A=45-56.
DR   PDBsum; 1IXU; -.
DR   AlphaFoldDB; P29399; -.
DR   SMR; P29399; -.
DR   MEROPS; I10.001; -.
DR   EvolutionaryTrace; P29399; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR022217; Prot_inh_I10_marinostatin.
DR   Pfam; PF12559; Inhibitor_I10; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Protease inhibitor;
KW   Pyrrolidone carboxylic acid; Serine protease inhibitor; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:9972273"
FT   CHAIN           30..63
FT                   /note="Marinostatin-L"
FT                   /id="PRO_0000021651"
FT   PEPTIDE         43..56
FT                   /note="Marinostatin-C2"
FT                   /id="PRO_0000021652"
FT   PEPTIDE         45..56
FT                   /note="Marinostatin-C1"
FT                   /id="PRO_0000021653"
FT   PEPTIDE         46..56
FT                   /note="Marinostatin-D"
FT                   /id="PRO_0000021654"
FT   REGION          23..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            48..49
FT                   /note="Reactive bond"
FT   MOD_RES         43
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:1794974"
FT   CONFLICT        54..55
FT                   /note="SD -> DS (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   63 AA;  6986 MW;  8E23AD74CEA9AE32 CRC64;
     MKTTPFFANL LASQTRELTE NELEMTAGGT ASQQSPVQEV PEQPFATMRY PSDSDEDGFN
     FPV