MLIC_YERE8
ID MLIC_YERE8 Reviewed; 117 AA.
AC P28837; A1JNW5;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Membrane-bound lysozyme inhibitor of C-type lysozyme {ECO:0000250|UniProtKB:P28224};
DE Flags: Precursor;
GN Name=mliC; OrderedLocusNames=YE2141 {ECO:0000312|EMBL:CAL12211.1};
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101.
RC STRAIN=ATCC 51872 / WA-C / Serotype O:8;
RA Baeumler A.J.;
RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
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}.
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; AM286415; CAL12211.1; -; Genomic_DNA.
DR EMBL; X60449; CAA42979.1; -; Genomic_DNA.
DR RefSeq; WP_011816373.1; NC_008800.1.
DR RefSeq; YP_001006381.1; NC_008800.1.
DR AlphaFoldDB; P28837; -.
DR SMR; P28837; -.
DR STRING; 393305.YE2141; -.
DR EnsemblBacteria; CAL12211; CAL12211; YE2141.
DR KEGG; yen:YE2141; -.
DR PATRIC; fig|393305.7.peg.2304; -.
DR eggNOG; COG3895; Bacteria.
DR HOGENOM; CLU_166586_0_0_6; -.
DR OMA; EYRCDEK; -.
DR Proteomes; UP000000642; 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..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..117
FT /note="Membrane-bound lysozyme inhibitor of C-type
FT lysozyme"
FT /id="PRO_0000066375"
FT SITE 70
FT /note="Directly involved in lysozyme active site
FT inhibition"
FT /evidence="ECO:0000250|UniProtKB:Q9I574"
FT SITE 84
FT /note="Directly involved in lysozyme active site
FT inhibition"
FT /evidence="ECO:0000250|UniProtKB:Q9I574"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT DISULFID 36..101
FT /evidence="ECO:0000250|UniProtKB:P28224"
SQ SEQUENCE 117 AA; 12901 MW; 0CBF9472E4FFF9C4 CRC64;
MKHLFGTTAV LGTAAVLMLT GCSLVQPKNE TLHYQCGGTK LTVMQDNKQD KVSLVLDGKQ
LTLPQVRAAS GAKYSDNHYT FWSKGNTAFV ERDEKVIIND CRLLTTPNDS ILQGEDR