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   24-JAN-2024, entry version 115.
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; Pseudomonadota; 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}.
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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   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   AlphaFoldDB; P0AD59; -.
DR   SMR; P0AD59; -.
DR   BioGRID; 4261212; 10.
DR   DIP; DIP-10051N; -.
DR   IntAct; P0AD59; 1.
DR   STRING; 511145.b0220; -.
DR   jPOST; P0AD59; -.
DR   PaxDb; 511145-b0220; -.
DR   EnsemblBacteria; AAC73324; AAC73324; b0220.
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   OMA; HDCAAQN; -.
DR   OrthoDB; 9033596at2; -.
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:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR   Gene3D; 3.40.1420.10; Inhibitor of vertebrate lysozyme; 1.
DR   InterPro; IPR036501; Inhibitor_vert_lysozyme_sf.
DR   InterPro; IPR014453; Inhibitor_vertebrate_lysozyme.
DR   Pfam; PF08816; Ivy; 1.
DR   PIRSF; PIRSF009103; Ivy; 1.
DR   SUPFAM; SSF89872; Inhibitor of vertebrate lysozyme, Ivy; 1.
DR   SWISS-2DPAGE; P0AD59; -.
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:0007829|PDB:1XS0"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   HELIX           44..51
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   HELIX           59..62
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   STRAND          65..75
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   STRAND          77..85
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   STRAND          93..99
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   STRAND          106..113
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:1GPQ"
FT   HELIX           133..144
FT                   /evidence="ECO:0007829|PDB:1XS0"
FT   HELIX           146..149
FT                   /evidence="ECO:0007829|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
//