MLIC_PSEAE
ID MLIC_PSEAE Reviewed; 127 AA.
AC Q9I574;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Membrane-bound lysozyme inhibitor of C-type lysozyme {ECO:0000303|PubMed:19028453};
DE Flags: Precursor;
GN Name=mliC {ECO:0000303|PubMed:19028453}; OrderedLocusNames=PA0867;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 31-127 IN COMPLEX WITH CHICKEN
RP LYSOZYME, FUNCTION, SUBUNIT, MUTAGENESIS OF SER-89 AND LYS-103, AND
RP DISULFIDE BOND.
RX PubMed=19028453; DOI=10.1016/j.bbrc.2008.11.039;
RA Yum S., Kim M.J., Xu Y., Jin X.L., Yoo H.Y., Park J.-W., Gong J.H.,
RA Choe K.-M., Lee B.L., Ha N.-C.;
RT "Structural basis for the recognition of lysozyme by MliC, a periplasmic
RT lysozyme inhibitor in Gram-negative bacteria.";
RL Biochem. Biophys. Res. Commun. 378:244-248(2009).
CC -!- FUNCTION: Specifically inhibits C-type lysozymes.
CC {ECO:0000269|PubMed:19028453}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:19028453}.
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 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG04256.1; -; Genomic_DNA.
DR PIR; H83537; H83537.
DR RefSeq; NP_249558.1; NC_002516.2.
DR RefSeq; WP_003085889.1; NZ_QZGE01000007.1.
DR PDB; 3F6Z; X-ray; 2.50 A; B/D=29-127.
DR PDBsum; 3F6Z; -.
DR AlphaFoldDB; Q9I574; -.
DR SMR; Q9I574; -.
DR STRING; 287.DR97_1076; -.
DR PaxDb; Q9I574; -.
DR PRIDE; Q9I574; -.
DR DNASU; 882238; -.
DR EnsemblBacteria; AAG04256; AAG04256; PA0867.
DR GeneID; 882238; -.
DR KEGG; pae:PA0867; -.
DR PATRIC; fig|208964.12.peg.901; -.
DR PseudoCAP; PA0867; -.
DR HOGENOM; CLU_151151_0_0_6; -.
DR InParanoid; Q9I574; -.
DR OMA; NEVTLYD; -.
DR PhylomeDB; Q9I574; -.
DR BioCyc; PAER208964:G1FZ6-882-MON; -.
DR EvolutionaryTrace; Q9I574; -.
DR Proteomes; UP000002438; 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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Disulfide bond; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..127
FT /note="Membrane-bound lysozyme inhibitor of C-type
FT lysozyme"
FT /id="PRO_0000378110"
FT SITE 89
FT /note="Directly involved in lysozyme active site
FT inhibition"
FT /evidence="ECO:0000305|PubMed:19028453"
FT SITE 103
FT /note="Directly involved in lysozyme active site
FT inhibition"
FT /evidence="ECO:0000305|PubMed:19028453"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT DISULFID 51..124
FT /evidence="ECO:0000269|PubMed:19028453"
FT MUTAGEN 89
FT /note="S->A: Significantly reduced inhibitory activity."
FT /evidence="ECO:0000269|PubMed:19028453"
FT MUTAGEN 103
FT /note="K->A: Significantly reduced inhibitory activity."
FT /evidence="ECO:0000269|PubMed:19028453"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:3F6Z"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:3F6Z"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:3F6Z"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:3F6Z"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:3F6Z"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3F6Z"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3F6Z"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3F6Z"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3F6Z"
SQ SEQUENCE 127 AA; 13695 MW; 70DDB95ABB6371AD CRC64;
MKKALWLLLA AVPVVLVACG GSDDDKQTAQ VDYLALPGDA KLDTRSVDYK CENGRKFTVQ
YLNKGDNSLA VVPVSDNSTL VFSNVISASG AKYAAGQYIW WTKGEEATLY GDWKGGEPTD
GVACKER
