ID   IPI_BACSU               Reviewed;         119 AA.
AC   P39804;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Intracellular proteinase inhibitor;
DE   AltName: Full=BsuPI;
GN   Name=ipi; OrderedLocusNames=BSU11130;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC   STRAIN=168 / DB104;
RX   PubMed=8226659; DOI=10.1128/jb.175.22.7130-7137.1993;
RA   Shiga Y., Yamagata H., Udaka S.;
RT   "Characterization of the gene encoding an intracellular proteinase
RT   inhibitor of Bacillus subtilis and its role in regulation of the major
RT   intracellular proteinase.";
RL   J. Bacteriol. 175:7130-7137(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9025291; DOI=10.1099/00221287-143-1-175;
RA   Levine A., Vannier F., Roche B., Autret S., Mavel D., Seror S.J.;
RT   "A 10.3 kbp segment from nprB to argJ at the 102 degrees region of the
RT   Bacillus subtilis chromosome.";
RL   Microbiology 143:175-177(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA   Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT   "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT   degrees) in Bacillus subtilis.";
RL   Microbiology 143:3305-3308(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Directly regulates the major intracellular proteinase (ISP-1)
CC       activity in vivo. Inhibits ISP-1 in the early stages of sporulation. It
CC       may be then inactivated by a membrane-bound proteinase.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D16311; BAA03820.1; -; Genomic_DNA.
DR   EMBL; Z79580; CAB01835.1; -; Genomic_DNA.
DR   EMBL; Y09476; CAA70631.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12953.1; -; Genomic_DNA.
DR   PIR; C49921; C49921.
DR   RefSeq; NP_388994.1; NC_000964.3.
DR   RefSeq; WP_010886475.1; NZ_JNCM01000035.1.
DR   PDB; 3ISY; X-ray; 2.61 A; A=1-119.
DR   PDBsum; 3ISY; -.
DR   AlphaFoldDB; P39804; -.
DR   BMRB; P39804; -.
DR   SMR; P39804; -.
DR   IntAct; P39804; 1.
DR   STRING; 224308.BSU11130; -.
DR   MEROPS; I22.001; -.
DR   PaxDb; P39804; -.
DR   DNASU; 936380; -.
DR   EnsemblBacteria; CAB12953; CAB12953; BSU_11130.
DR   GeneID; 936380; -.
DR   KEGG; bsu:BSU11130; -.
DR   PATRIC; fig|224308.43.peg.1160; -.
DR   eggNOG; ENOG50339GZ; Bacteria.
DR   OMA; ERYRYSK; -.
DR   BioCyc; BSUB:BSU11130-MON; -.
DR   EvolutionaryTrace; P39804; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.2360; -; 1.
DR   InterPro; IPR020481; Intracell_prot_inh_BsuPI.
DR   InterPro; IPR038144; IPI.
DR   Pfam; PF12690; BsuPI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Protease inhibitor;
KW   Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..119
FT                   /note="Intracellular proteinase inhibitor"
FT                   /id="PRO_0000084223"
FT   STRAND          5..14
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   STRAND          19..27
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   STRAND          33..40
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   STRAND          43..48
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   TURN            58..61
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   STRAND          78..87
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   STRAND          91..100
FT                   /evidence="ECO:0007829|PDB:3ISY"
FT   STRAND          111..118
FT                   /evidence="ECO:0007829|PDB:3ISY"
SQ   SEQUENCE   119 AA;  14074 MW;  DDACBCA16C721308 CRC64;
     MENQEVVLSI DAIQEPEQIK FNMSLKNQSE RAIEFQFSTG QKFELVVYDS EHKERYRYSK
     EKMFTQAFQN LTLESGETYD FSDVWKEVPE PGTYEVKVTF KGRAENLKQV QAVQQFEVK