MLTC_YERE8
ID MLTC_YERE8 Reviewed; 358 AA.
AC A1JPV7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 86.
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=YE3445;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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=CAL13469.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM286415; CAL13469.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_005157159.1; NC_008800.1.
DR RefSeq; YP_001007611.1; NC_008800.1.
DR AlphaFoldDB; A1JPV7; -.
DR SMR; A1JPV7; -.
DR STRING; 393305.YE3445; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; CAL13469; CAL13469; YE3445.
DR GeneID; 67420173; -.
DR KEGG; yen:YE3445; -.
DR PATRIC; fig|393305.7.peg.3659; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_044583_0_0_6; -.
DR Proteomes; UP000000642; 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..358
FT /note="Membrane-bound lytic murein transglycosylase C"
FT /id="PRO_0000323521"
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; 39786 MW; 7CE9497981BACDFF CRC64;
MKKILALLVI APLLVSCSGN KNQADNEAFI KDTNGFEILM GQFAHNIENI WGLKEVLIAG
PKDYVKYTDQ YQTRSHINFD AGTITVETIA TTDPAAHLRQ AIITTLLMGD DPGSIDLYSD
ANDIQISKEP FLYGQVLDNN GEPIRWEWRA AHFADYLLQN KMQKRTSGLH VIWSVTLQLV
PNHLDKRAHK YLPLVRQSAE KYGVEESLIL AIMQTESSFN PYAVSGSDAL GLMQVVQHTA
GRDVFKMKGK SGQPSRSYLF DPANNIDAGT AYLSILQNTY LGGIQNATSR RYAVITSYNG
GAGSVLRVFS SDKNQAVNII NNMAPGDVFQ TLTTKHPSGE SRRYLVKVNS AQKSYRRH