ID   MLIC_CROS8              Reviewed;         107 AA.
AC   A7MMK4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Membrane-bound lysozyme inhibitor of C-type lysozyme {ECO:0000250|UniProtKB:P28224};
DE   Flags: Precursor;
GN   Name=mliC; OrderedLocusNames=ESA_01998;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- FUNCTION: Specifically inhibits C-type lysozymes.
CC       {ECO:0000250|UniProtKB:P28224}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P28224}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000250|UniProtKB:P28224}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}. Note=Anchored to the periplasmic side.
CC       {ECO:0000250|UniProtKB:P28224}.
CC   -!- SIMILARITY: Belongs to the MliC family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000783; ABU77251.1; -; Genomic_DNA.
DR   RefSeq; WP_004386093.1; NC_009778.1.
DR   AlphaFoldDB; A7MMK4; -.
DR   SMR; A7MMK4; -.
DR   EnsemblBacteria; ABU77251; ABU77251; ESA_01998.
DR   GeneID; 56730771; -.
DR   KEGG; esa:ESA_01998; -.
DR   HOGENOM; CLU_166586_0_0_6; -.
DR   OMA; EYRCDEK; -.
DR   OrthoDB; 1987224at2; -.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.40.128.200; -; 1.
DR   InterPro; IPR018660; MliC.
DR   InterPro; IPR036328; MliC_sf.
DR   Pfam; PF09864; MliC; 1.
DR   SUPFAM; SSF141488; SSF141488; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Disulfide bond; Lipoprotein; Membrane; Palmitate;
KW   Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           16..107
FT                   /note="Membrane-bound lysozyme inhibitor of C-type
FT                   lysozyme"
FT                   /id="PRO_0000378109"
FT   SITE            69
FT                   /note="Directly involved in lysozyme active site
FT                   inhibition"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I574"
FT   SITE            83
FT                   /note="Directly involved in lysozyme active site
FT                   inhibition"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I574"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   DISULFID        35..100
FT                   /evidence="ECO:0000250|UniProtKB:P28224"
SQ   SEQUENCE   107 AA;  12355 MW;  6367700530D9576D CRC64;
     MKKLLVVLLP TLLAGCSYYD AMVERMNTDT LEYRCDEKPL TVSLNKQREQ VSFVLDDKML
     HLNQGRAASG TRYTDGIYAF WSKGDEATVY HRDNIVLNHC QLQNPKR