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MLIC_ECOLI
ID   MLIC_ECOLI              Reviewed;         109 AA.
AC   P28224;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Membrane-bound lysozyme inhibitor of C-type lysozyme {ECO:0000303|PubMed:18369469};
DE   Flags: Precursor;
GN   Name=mliC {ECO:0000303|PubMed:18369469}; Synonyms=ydhA;
GN   OrderedLocusNames=b1639, JW1631;
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;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-109.
RC   STRAIN=K12;
RX   PubMed=1356963; DOI=10.1128/jb.174.19.6033-6045.1992;
RA   Lam H.-M., Winkler M.E.;
RT   "Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12
RT   and pleiotropic phenotypes caused by pdxH insertion mutations.";
RL   J. Bacteriol. 174:6033-6045(1992).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18369469; DOI=10.1371/journal.ppat.1000019;
RA   Callewaert L., Aertsen A., Deckers D., Vanoirbeek K.G., Vanderkelen L.,
RA   Van Herreweghe J.M., Masschalck B., Nakimbugwe D., Robben J.,
RA   Michiels C.W.;
RT   "A new family of lysozyme inhibitors contributing to lysozyme tolerance in
RT   Gram-negative bacteria.";
RL   PLoS Pathog. 4:E1000019-E1000019(2008).
RN   [6]
RP   STRUCTURE BY NMR OF 28-109, SUBUNIT, AND DISULFIDE BOND.
RX   PubMed=16937244; DOI=10.1007/s10858-006-9032-y;
RA   Revington M., Semesi A., Yee A., Arrowsmith C.H., Shaw G.S.;
RT   "The solution structure of the protein ydhA from Escherichia coli.";
RL   J. Biomol. NMR 35:295-300(2006).
CC   -!- FUNCTION: Specifically inhibits C-type lysozymes.
CC       {ECO:0000269|PubMed:18369469}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16937244}.
CC   -!- INTERACTION:
CC       P28224; P0ACG8: hslR; NbExp=3; IntAct=EBI-562851, EBI-562824;
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000269|PubMed:18369469}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000269|PubMed:18369469}. Note=Anchored to the
CC       periplasmic side. {ECO:0000269|PubMed:18369469}.
CC   -!- SIMILARITY: Belongs to the MliC family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC74711.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15400.2; -; Genomic_DNA.
DR   EMBL; M92351; AAA24708.1; -; Genomic_DNA.
DR   PIR; A43261; A43261.
DR   RefSeq; NP_416156.4; NC_000913.3.
DR   RefSeq; WP_000178044.1; NZ_STEB01000003.1.
DR   PDB; 2F09; NMR; -; A=28-109.
DR   PDBsum; 2F09; -.
DR   AlphaFoldDB; P28224; -.
DR   SMR; P28224; -.
DR   BioGRID; 4263489; 136.
DR   BioGRID; 851152; 1.
DR   DIP; DIP-11726N; -.
DR   IntAct; P28224; 5.
DR   STRING; 511145.b1639; -.
DR   jPOST; P28224; -.
DR   PaxDb; P28224; -.
DR   PRIDE; P28224; -.
DR   EnsemblBacteria; AAC74711; AAC74711; b1639.
DR   EnsemblBacteria; BAA15400; BAA15400; BAA15400.
DR   GeneID; 946811; -.
DR   KEGG; ecj:JW1631; -.
DR   KEGG; eco:b1639; -.
DR   PATRIC; fig|511145.12.peg.1710; -.
DR   EchoBASE; EB1451; -.
DR   eggNOG; COG3895; Bacteria.
DR   HOGENOM; CLU_166586_0_0_6; -.
DR   InParanoid; P28224; -.
DR   OMA; EYRCDEK; -.
DR   PhylomeDB; P28224; -.
DR   BioCyc; EcoCyc:EG11488-MON; -.
DR   EvolutionaryTrace; P28224; -.
DR   PRO; PR:P28224; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR   GO; GO:0060241; F:lysozyme inhibitor activity; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   3D-structure; Cell outer membrane; Disulfide bond; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           18..109
FT                   /note="Membrane-bound lysozyme inhibitor of C-type
FT                   lysozyme"
FT                   /id="PRO_0000168974"
FT   SITE            71
FT                   /note="Directly involved in lysozyme active site
FT                   inhibition"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I574"
FT   SITE            85
FT                   /note="Directly involved in lysozyme active site
FT                   inhibition"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I574"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   DISULFID        37..102
FT                   /evidence="ECO:0000269|PubMed:16937244"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:2F09"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:2F09"
FT   STRAND          50..66
FT                   /evidence="ECO:0007829|PDB:2F09"
FT   STRAND          70..76
FT                   /evidence="ECO:0007829|PDB:2F09"
FT   STRAND          81..84
FT                   /evidence="ECO:0007829|PDB:2F09"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:2F09"
FT   STRAND          97..100
FT                   /evidence="ECO:0007829|PDB:2F09"
SQ   SEQUENCE   109 AA;  12568 MW;  FB6E5F97F6893224 CRC64;
     MTMKKLLIII LPVLLSGCSA FNQLVERMQT DTLEYQCDEK PLTVKLNNPR QEVSFVYDNQ
     LLHLKQGISA SGARYTDGIY VFWSKGDEAT VYKRDRIVLN NCQLQNPQR
 
 
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