ID IVY_ECOLI Reviewed; 157 AA. AC P0AD59; P45502; P77185; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 07-OCT-2020, entry version 102. DE RecName: Full=Inhibitor of vertebrate lysozyme; DE Flags: Precursor; GN Name=ivy; Synonyms=ykfE; OrderedLocusNames=b0220, JW0210; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 RT - 6.0 min (189,987 - 281,416bp) region."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP PROTEIN SEQUENCE OF 29-39. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.; RL Submitted (AUG-1995) to UniProtKB. RN [6] RP PROTEIN SEQUENCE OF 29-38. RC STRAIN=K12; RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x; RA Wasinger V.C., Humphery-Smith I.; RT "Small genes/gene-products in Escherichia coli K-12."; RL FEMS Microbiol. Lett. 169:375-382(1998). RN [7] RP CHARACTERIZATION. RC STRAIN=K12 / XL1-Blue; RX PubMed=11278658; DOI=10.1074/jbc.m010297200; RA Montchois V., Abergel C., Sturgis J., Jeudy S., Claverie J.-M.; RT "Escherichia coli ykfE ORFan gene encodes a potent inhibitor of C-type RT lysozyme."; RL J. Biol. Chem. 276:18437-18441(2001). RN [8] RP CRYSTALLIZATION. RX PubMed=11092949; DOI=10.1107/s0907444900015316; RA Abergel C., Monchois V., Chenivesse S., Jeudy S., Claverie J.-M.; RT "Crystallization and preliminary crystallographic study of b0220, an RT 'ORFan' protein of unknown function from Escherichia coli."; RL Acta Crystallogr. D 56:1694-1695(2000). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RA Abergel C., Monchois V., Claverie J.-M.; RT "Structure and evolution of a paradoxical protein family of vertebrate RT lysozyme inhibitors only found in Gram-negative bacteria."; RL Submitted (NOV-2001) to the PDB data bank. CC -!- FUNCTION: Strong inhibitor of lysozyme C. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the ivy family. {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; U70214; AAB08642.1; -; Genomic_DNA. DR EMBL; U00096; AAC73324.1; -; Genomic_DNA. DR EMBL; AP009048; BAA77890.1; -; Genomic_DNA. DR PIR; E64746; E64746. DR RefSeq; NP_414755.1; NC_000913.3. DR RefSeq; WP_000532698.1; NZ_STEB01000020.1. DR PDB; 1GPQ; X-ray; 1.60 A; A/B=29-156. DR PDB; 1XS0; X-ray; 1.58 A; A/B/C=29-156. DR PDBsum; 1GPQ; -. DR PDBsum; 1XS0; -. DR SMR; P0AD59; -. DR BioGRID; 4261212; 10. DR DIP; DIP-10051N; -. DR IntAct; P0AD59; 1. DR STRING; 511145.b0220; -. DR SWISS-2DPAGE; P0AD59; -. DR jPOST; P0AD59; -. DR PaxDb; P0AD59; -. DR PRIDE; P0AD59; -. DR EnsemblBacteria; AAC73324; AAC73324; b0220. DR EnsemblBacteria; BAA77890; BAA77890; BAA77890. DR GeneID; 48136914; -. DR GeneID; 946530; -. DR KEGG; ecj:JW0210; -. DR KEGG; eco:b0220; -. DR PATRIC; fig|1411691.4.peg.2063; -. DR EchoBASE; EB3317; -. DR eggNOG; ENOG50305HJ; Bacteria. DR HOGENOM; CLU_109262_0_0_6; -. DR InParanoid; P0AD59; -. DR BioCyc; EcoCyc:G6104-MONOMER; -. DR EvolutionaryTrace; P0AD59; -. DR PRO; PR:P0AD59; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc. DR GO; GO:0060241; F:lysozyme inhibitor activity; IDA:EcoCyc. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc. DR GO; GO:0050790; P:regulation of catalytic activity; IDA:EcoCyc. DR Gene3D; 3.40.1420.10; -; 1. DR InterPro; IPR036501; Inhibitor_vert_lysozyme_sf. DR InterPro; IPR014453; Inhibitor_vertebrate_lysozyme. DR PIRSF; PIRSF009103; Ivy; 1. DR SUPFAM; SSF89872; SSF89872; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Periplasm; KW Reference proteome; Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000269|PubMed:9868784, ECO:0000269|Ref.5" FT CHAIN 29..157 FT /note="Inhibitor of vertebrate lysozyme" FT /id="PRO_0000016546" FT SITE 88 FT /note="Important for lysozyme inhibition" FT DISULFID 85..90 FT CONFLICT 36 FT /note="Missing (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 34..39 FT /evidence="ECO:0000244|PDB:1XS0" FT TURN 41..43 FT /evidence="ECO:0000244|PDB:1XS0" FT HELIX 44..51 FT /evidence="ECO:0000244|PDB:1XS0" FT HELIX 59..62 FT /evidence="ECO:0000244|PDB:1XS0" FT STRAND 65..75 FT /evidence="ECO:0000244|PDB:1XS0" FT STRAND 77..85 FT /evidence="ECO:0000244|PDB:1XS0" FT TURN 90..92 FT /evidence="ECO:0000244|PDB:1XS0" FT STRAND 93..99 FT /evidence="ECO:0000244|PDB:1XS0" FT TURN 101..103 FT /evidence="ECO:0000244|PDB:1XS0" FT STRAND 106..113 FT /evidence="ECO:0000244|PDB:1XS0" FT TURN 115..117 FT /evidence="ECO:0000244|PDB:1XS0" FT STRAND 120..125 FT /evidence="ECO:0000244|PDB:1XS0" FT HELIX 129..131 FT /evidence="ECO:0000244|PDB:1GPQ" FT HELIX 133..144 FT /evidence="ECO:0000244|PDB:1XS0" FT HELIX 146..149 FT /evidence="ECO:0000244|PDB:1XS0" SQ SEQUENCE 157 AA; 16872 MW; 9156C5944DFE6D84 CRC64; MGRISSGGMM FKAITTVAAL VIATSAMAQD DLTISSLAKG ETTKAAFNQM VQGHKLPAWV MKGGTYTPAQ TVTLGDETYQ VMSACKPHDC GSQRIAVMWS EKSNQMTGLF STIDEKTSQE KLTWLNVNDA LSIDGKTVLF AALTGSLENH PDGFNFK //