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MLTC_SALTY
ID   MLTC_SALTY              Reviewed;         360 AA.
AC   Q8ZM39;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   25-MAY-2022, entry version 106.
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=STM3112;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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=AAL21987.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006468; AAL21987.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_462028.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZM39; -.
DR   SMR; Q8ZM39; -.
DR   STRING; 99287.STM3112; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   PaxDb; Q8ZM39; -.
DR   EnsemblBacteria; AAL21987; AAL21987; STM3112.
DR   GeneID; 1254635; -.
DR   KEGG; stm:STM3112; -.
DR   PATRIC; fig|99287.12.peg.3298; -.
DR   HOGENOM; CLU_044583_0_0_6; -.
DR   OMA; AIMQIES; -.
DR   PhylomeDB; Q8ZM39; -.
DR   Proteomes; UP000001014; 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..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT   CHAIN           17..360
FT                   /note="Membrane-bound lytic murein transglycosylase C"
FT                   /id="PRO_0000032797"
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   360 AA;  40275 MW;  6A0EB5627275B8AC CRC64;
     MKKLLALAVI APLLISCSSS TKKGETYNEA WVKDTNGFDI LMGQFANNIE NLWGYKEVLI
     AGPKDYVKYT DQFQTRSHIN FDDGTITVET IAGTEPTAHL RRAIIKTLLM GDDPTSVDLY
     SDVDDIKISK EPFLYGQVLD NTGQPIRWEG RATTFADYLL KTRLKSRSNG LRIIYSVTIN
     LVPNHLDKRA HKYIGMVRQA SRKYGVDESL ILAIMQTESS FNPYAVSHAD ALGLMQVVQH
     SAGKDVFRSQ GKSGTPSRNF LFDPASNIDT GTAYLAMLNN VYLSGIENPT SRRYAVITAY
     NGGAGSVLRV FSNDKIQAAN MINRMSPGDV YQILTTRHPS AESRRYLYKV NSAQRSYRRR
 
 
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