ID   MLTC_YERPG              Reviewed;         358 AA.
AC   A9R6R2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase C {ECO:0000255|HAMAP-Rule:MF_01616};
DE            EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_01616};
DE   AltName: Full=Murein lyase C {ECO:0000255|HAMAP-Rule:MF_01616};
DE   Flags: Precursor;
GN   Name=mltC {ECO:0000255|HAMAP-Rule:MF_01616};
GN   OrderedLocusNames=YpAngola_A0153;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division.
CC       {ECO:0000255|HAMAP-Rule:MF_01616}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC         non-reducing ends of the peptidoglycan chains, with concomitant
CC         formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01616};
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01616}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01616}.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000255|HAMAP-Rule:MF_01616}.
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DR   EMBL; CP000901; ABX86561.1; -; Genomic_DNA.
DR   RefSeq; WP_002209995.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R6R2; -.
DR   SMR; A9R6R2; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   GeneID; 66844343; -.
DR   KEGG; ypg:YpAngola_A0153; -.
DR   PATRIC; fig|349746.12.peg.1094; -.
DR   OMA; AIMQIES; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   HAMAP; MF_01616; MltC; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR023664; Murein_transglycosylaseC.
DR   InterPro; IPR024570; Murein_transglycosylaseC_N.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF11873; Mltc_N; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell wall biogenesis/degradation; Lipoprotein; Lyase;
KW   Membrane; Palmitate; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT   CHAIN           17..358
FT                   /note="Membrane-bound lytic murein transglycosylase C"
FT                   /id="PRO_1000185933"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
SQ   SEQUENCE   358 AA;  39947 MW;  DA79BBFD6951C952 CRC64;
     MKKILALLVI APLLVSCSGN KNQVENEVFV KDTNGFEILM GQFAHNIENI WGLKEVLIAG
     PKDYVKYTDQ YQTRSHINFD AGTITIETIA TTNPAAHLRQ AIITTLLMGD DPGSIDLYSD
     VNDIQISKEP FLYGQVLDNN GEPIRWEWRA AHFADYLLQN KMQTRTSGLH VISFVTIQLV
     PNHLDKRAHK YLPLVRKSAA RYGVEESLIL AIMQTESSFN PYAVSRSDAL GLMQVVQHTA
     GKDVFKLKGK SGQPSRSYLF DPENNIDAGT AYLSILQNTY LGGIQNATSR RYAVITSYNG
     GAGSVLRVFH SDKNKAVGII NTMSPGDVFQ TLTTKHPSGE SRRYLVKVNS AQKNYRRY