INH_PSEAE
ID INH_PSEAE Reviewed; 131 AA.
AC Q03026;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Proteinase inhibitor;
DE AltName: Full=Aprin;
DE Flags: Precursor;
GN Name=inh; Synonyms=aprI; OrderedLocusNames=PA1250;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1427098; DOI=10.1016/0378-1119(92)90160-q;
RA Duong F., Lazdunski A., Cami B., Murgier M.;
RT "Sequence of a cluster of genes controlling synthesis and secretion of
RT alkaline protease in Pseudomonas aeruginosa: relationships to other
RT secretory pathways.";
RL Gene 121:47-54(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH PROTEASE.
RX PubMed=11445573; DOI=10.1074/jbc.m104020200;
RA Hege T., Feltzer R.E., Gray R.D., Baumann U.;
RT "Crystal structure of a complex between Pseudomonas aeruginosa alkaline
RT protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative
RT bond.";
RL J. Biol. Chem. 276:35087-35092(2001).
CC -!- FUNCTION: Inhibitor of the alkaline protease. It forms a non-covalent
CC bond with the protease and may prevent its autocatalytic cleavage in
CC the periplasm (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the protease inhibitor I38 family.
CC {ECO:0000305}.
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; X64558; CAA45859.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04639.1; -; Genomic_DNA.
DR PIR; S26700; S26700.
DR RefSeq; NP_249941.1; NC_002516.2.
DR RefSeq; WP_003082543.1; NC_002516.2.
DR PDB; 1JIW; X-ray; 1.74 A; I=26-131.
DR PDB; 2RN4; NMR; -; A=26-131.
DR PDBsum; 1JIW; -.
DR PDBsum; 2RN4; -.
DR AlphaFoldDB; Q03026; -.
DR BMRB; Q03026; -.
DR SMR; Q03026; -.
DR MINT; Q03026; -.
DR STRING; 287.DR97_687; -.
DR MEROPS; I38.002; -.
DR PaxDb; Q03026; -.
DR PRIDE; Q03026; -.
DR DNASU; 881261; -.
DR EnsemblBacteria; AAG04639; AAG04639; PA1250.
DR GeneID; 881261; -.
DR KEGG; pae:PA1250; -.
DR PATRIC; fig|208964.12.peg.1298; -.
DR PseudoCAP; PA1250; -.
DR HOGENOM; CLU_155270_1_0_6; -.
DR OMA; PEGSIWS; -.
DR BioCyc; PAER208964:G1FZ6-1275-MON; -.
DR EvolutionaryTrace; Q03026; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR022815; Inh.
DR InterPro; IPR021140; Inh/Omp19.
DR InterPro; IPR016085; Protease_inh_b-brl_dom.
DR Pfam; PF02974; Inh; 1.
DR PRINTS; PR01274; MPTASEINHBTR.
DR SUPFAM; SSF50882; SSF50882; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Periplasm; Protease inhibitor;
KW Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..131
FT /note="Proteinase inhibitor"
FT /id="PRO_0000026717"
FT DISULFID 51..74
FT /evidence="ECO:0000250"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:1JIW"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:1JIW"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2RN4"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1JIW"
SQ SEQUENCE 131 AA; 13980 MW; 8CE4A64ED10AA8CD CRC64;
MSASAKLSRM VCLLCGFFST GISMASSLIL LSASDLAGQW TLQQDEAPAI CHLELRDSEV
AEASGYDLGG DTACLTRWLP SEPRAWRPTP AGIALLERGG LTLMLLGRQG EGDYRVQKGD
GGQLVLRRAT P
