ECOT_PSEPK
ID ECOT_PSEPK Reviewed; 159 AA.
AC Q88IC7;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Ecotin {ECO:0000255|HAMAP-Rule:MF_00706};
DE Flags: Precursor;
GN Name=eco {ECO:0000255|HAMAP-Rule:MF_00706}; OrderedLocusNames=PP_3072;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: General inhibitor of family S1 serine proteases.
CC {ECO:0000255|HAMAP-Rule:MF_00706}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00706}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00706}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I11 (ecotin) family.
CC {ECO:0000255|HAMAP-Rule:MF_00706}.
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DR EMBL; AE015451; AAN68680.1; -; Genomic_DNA.
DR RefSeq; NP_745216.1; NC_002947.4.
DR RefSeq; WP_010953971.1; NC_002947.4.
DR AlphaFoldDB; Q88IC7; -.
DR SMR; Q88IC7; -.
DR STRING; 160488.PP_3072; -.
DR MEROPS; I11.003; -.
DR PRIDE; Q88IC7; -.
DR EnsemblBacteria; AAN68680; AAN68680; PP_3072.
DR KEGG; ppu:PP_3072; -.
DR PATRIC; fig|160488.4.peg.3245; -.
DR eggNOG; COG4574; Bacteria.
DR HOGENOM; CLU_111565_0_0_6; -.
DR OMA; PKAEKGM; -.
DR PhylomeDB; Q88IC7; -.
DR BioCyc; PPUT160488:G1G01-3265-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-UniRule.
DR CDD; cd00242; Ecotin; 1.
DR Gene3D; 4.10.1230.10; -; 1.
DR HAMAP; MF_00706; Ecotin; 1.
DR InterPro; IPR027438; Ecotin_C.
DR InterPro; IPR036198; Ecotin_sf.
DR InterPro; IPR005658; Prot_inh_ecotin.
DR InterPro; IPR023084; Prot_inh_ecotin_gammaproteobac.
DR PANTHER; PTHR35890; PTHR35890; 1.
DR Pfam; PF03974; Ecotin; 1.
DR PIRSF; PIRSF006865; Prot_inh_ecotin; 1.
DR SUPFAM; SSF49772; SSF49772; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Periplasm; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT CHAIN 23..159
FT /note="Ecotin"
FT /id="PRO_0000007428"
FT SITE 102..103
FT /note="Reactive bond"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
FT DISULFID 68..105
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00706"
SQ SEQUENCE 159 AA; 17382 MW; 4D21534D5044C453 CRC64;
MRPTPMTAIL ALSLAAAAPA MAASLKDIAP YPEAEKGFTR QVIHLPAQAD ESAYKLEILA
GKTLQVDCNR QRLGGNLEAH TLEGWGYNYY RLDNVSGPAS TLMACPDGKK TEAFVPVVGD
GFLLRYNSKL PVVVYVPKDV EVRYRVWSAS QDVQKAKVE
