ID   MLTC_PASMU              Reviewed;         358 AA.
AC   Q9CLB8;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   25-MAY-2022, entry version 109.
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}; OrderedLocusNames=PM1321;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK03405.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004439; AAK03405.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_016533805.1; NC_002663.1.
DR   AlphaFoldDB; Q9CLB8; -.
DR   SMR; Q9CLB8; -.
DR   STRING; 747.DR93_569; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   PRIDE; Q9CLB8; -.
DR   EnsemblBacteria; AAK03405; AAK03405; PM1321.
DR   KEGG; pmu:PM1321; -.
DR   PATRIC; fig|272843.6.peg.1332; -.
DR   HOGENOM; CLU_044583_0_0_6; -.
DR   OMA; AIMQIES; -.
DR   Proteomes; UP000000809; Chromosome.
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; Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT   CHAIN           16..358
FT                   /note="Membrane-bound lytic murein transglycosylase C"
FT                   /id="PRO_0000032792"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
SQ   SEQUENCE   358 AA;  40294 MW;  FA756EA47F4F23F6 CRC64;
     MKKYIIYALI PFLFACGGTK THRSSQFDEA FAKDTRGLDI LTGQFSHNID RIWGVNELLV
     ASRKDYVKYT DRFYTRSHVS FDEGLITVET QSDLRHLQNA IVHILLMGSD ANGIDLFASG
     DVPISSRPFL VGQVIDHLGG SITNTTTAGN FANYLLQNKL QTRRLSNGHT VQYVVIPMIA
     NHVAVRAQRY LPLVRKMARR YNMDESLILG IMQTESSFNP YAISYANAIG LMQVVPTTAG
     RDIFKMKGKG GQPSKSYLFD PEKNIDAGTS YLWLLQNKYL DGITNPTSKR FAMISAYNSG
     AGAVLRVFDQ DRDAAIVKIN SLYPEQVYRI LTTQHPSAQA RNYLLKVDQA QKSYRVRR