ID   MLTC_MANSM              Reviewed;         357 AA.
AC   Q65VT8;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   25-MAY-2022, entry version 93.
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=MS0315;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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=AAU36922.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016827; AAU36922.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041639491.1; NC_006300.1.
DR   AlphaFoldDB; Q65VT8; -.
DR   SMR; Q65VT8; -.
DR   STRING; 221988.MS0315; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; AAU36922; AAU36922; MS0315.
DR   KEGG; msu:MS0315; -.
DR   eggNOG; COG0741; Bacteria.
DR   HOGENOM; CLU_044583_0_0_6; -.
DR   OrthoDB; 1444566at2; -.
DR   Proteomes; UP000000607; 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; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT   CHAIN           18..357
FT                   /note="Membrane-bound lytic murein transglycosylase C"
FT                   /id="PRO_0000032791"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
SQ   SEQUENCE   357 AA;  40191 MW;  AB6B45969CB1E705 CRC64;
     MKLKKFLVLL LIPFLYACSS DRSGNYDDAF AKDTNGLDLL TGQFSQNIDQ IWGVNELLVA
     SRKDYVKYTD SYYTRSHISF EEGQITIETL ADANRLHSAI VHTLLMGSDA KGIDLFASGD
     VPISSRPFLV GQVVDNFGRQ INNIDVANSF ASYLLQNRLQ SRRLSNGRTV QFVSIQMIAN
     HVNVRARKYL SLVRQASRRY GIDESLILGI MQTESSFNPY AISYANAMGL MQVVPHTAGR
     DIFKLKGRSG QPSKSYLFDP ANNIDAGVSY LWILKNEYLA GITNPTSMRY AMISAYNSGA
     GAVLRVFDSD QEYAINIINR MQPEQVYRIL TTVHPSSQAR NYLLKVDKAQ RSYRRAR