MLTC_SALTI
ID MLTC_SALTI Reviewed; 360 AA.
AC Q8Z3T9; Q7C7A4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 25-MAY-2022, entry version 120.
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=STY3267, t3025;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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=AAO70577.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD02937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL513382; CAD02937.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014613; AAO70577.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_457505.1; NC_003198.1.
DR AlphaFoldDB; Q8Z3T9; -.
DR SMR; Q8Z3T9; -.
DR STRING; 220341.16504190; -.
DR EnsemblBacteria; AAO70577; AAO70577; t3025.
DR KEGG; stt:t3025; -.
DR KEGG; sty:STY3267; -.
DR PATRIC; fig|220341.7.peg.3332; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_044583_0_0_6; -.
DR OMA; AIMQIES; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01616"
FT CHAIN 17..360
FT /note="Membrane-bound lytic murein transglycosylase C"
FT /id="PRO_0000032796"
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; 40289 MW; 6A0EA2691FD468AC 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
NGGAGSVLRI FSNDKIQAAN MINRMSPGDV YQILTTRHPS AESRRYLYKV NSAQRSYRRR
