ID A0A0E1LZA0_ECOLX Unreviewed; 162 AA. AC A0A0E1LZA0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 05-JUN-2019, entry version 22. DE RecName: Full=Ecotin {ECO:0000256|HAMAP-Rule:MF_00706}; DE Flags: Precursor; GN Name=eco {ECO:0000256|HAMAP-Rule:MF_00706, GN ECO:0000313|EMBL:AJF57101.1}; GN ORFNames=EC1303_c23880 {ECO:0000313|EMBL:AJF57101.1}; OS Escherichia coli 1303. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=745156 {ECO:0000313|EMBL:AJF57101.1, ECO:0000313|Proteomes:UP000031758}; RN [1] {ECO:0000313|EMBL:AJF57101.1, ECO:0000313|Proteomes:UP000031758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1303 {ECO:0000313|EMBL:AJF57101.1, RC ECO:0000313|Proteomes:UP000031758}; RA Leimbach A., Poehlein A., Daniel R., Dobrindt U.; RT "Complete genome sequences of Escherichia coli strains 1303 and ECC- RT 1470 isolated from bovine mastitis."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: General inhibitor of pancreatic serine proteases: CC inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as CC well as a variety of other proteases. {ECO:0000256|HAMAP- CC Rule:MF_00706}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00706}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_00706}. CC -!- SIMILARITY: Belongs to the protease inhibitor I11 (ecotin) family. CC {ECO:0000256|HAMAP-Rule:MF_00706, ECO:0000256|SAAS:SAAS00959886}. 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; CP009166; AJF57101.1; -; Genomic_DNA. DR RefSeq; WP_000849209.1; NZ_CP009166.1. DR SMR; A0A0E1LZA0; -. DR EnsemblBacteria; AJF57101; AJF57101; EC1303_c23880. DR Proteomes; UP000031758; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. 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 Complete proteome {ECO:0000313|Proteomes:UP000031758}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00706}; KW Periplasm {ECO:0000256|HAMAP-Rule:MF_00706}; KW Protease inhibitor {ECO:0000256|HAMAP-Rule:MF_00706}; KW Serine protease inhibitor {ECO:0000256|HAMAP-Rule:MF_00706}; KW Signal {ECO:0000256|HAMAP-Rule:MF_00706}. FT SIGNAL 1 20 {ECO:0000256|HAMAP-Rule:MF_00706}. FT CHAIN 21 162 Ecotin. {ECO:0000256|HAMAP-Rule: FT MF_00706}. FT /FTId=PRO_5008986540. FT SITE 104 105 Reactive bond. {ECO:0000256|HAMAP-Rule: FT MF_00706}. FT DISULFID 70 107 {ECO:0000256|HAMAP-Rule:MF_00706}. SQ SEQUENCE 162 AA; 18192 MW; E965383177B92ECD CRC64; MKTILPAVLF AAFATTSAWA AESVQPLEKI APYPQAEKGM KRQVIQLTPQ EDESTLKVEL LIGQTLEVDC NLHRLGGKLE NKTLEGWGYD YYVFDKVSSP VSTMMACPDG KKEKKFVTAY LGDAGMLRYN SKLPIVVYTP DNVDVKYRVW KAEEKIDNAV VR //