MLTC_SHIDS
ID MLTC_SHIDS Reviewed; 359 AA.
AC Q32C32;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 25-MAY-2022, entry version 91.
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=SDY_3109;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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=ABB63123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000034; ABB63123.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_404614.1; NC_007606.1.
DR AlphaFoldDB; Q32C32; -.
DR SMR; Q32C32; -.
DR STRING; 300267.SDY_3109; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; ABB63123; ABB63123; SDY_3109.
DR KEGG; sdy:SDY_3109; -.
DR PATRIC; fig|300267.13.peg.3718; -.
DR HOGENOM; CLU_044583_0_0_6; -.
DR OMA; AIMQIES; -.
DR Proteomes; UP000002716; 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..359
FT /note="Membrane-bound lytic murein transglycosylase C"
FT /id="PRO_0000335588"
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 359 AA; 40112 MW; 3543FA42C36E1CA2 CRC64;
MKKYLALALI APLLISCSTT QKGDTYNEAW VKDTNGFDIL MGQFAHNIEN IWGFKEVVIA
GPKDYVKYTD QYQTRSHINF DDGTITIETI AGTEPAAHLR RAIIKTLLMG DDPSSVDLYS
DVDDITISKE PFLYGQVVDN TGQPIRWEGR ASNFADYLLK NRLKSRSNGL RIIYSVTINM
VPNHLDKRAH KYLGMVRQAS RKYGVDESLI LAIMQTESSF NPYAVSRSDA LGLMQVVQHT
AGKDVFRSQG KSGTPSRSFL FDPASNIDTG TAYLAMLNNV YLGGIDNPTS RRYAVITAYN
GGAGSVLRVF SNDKIQAANI INTMTPGDVY QTLTTRHPSA ESRRYLYKVN TAQKSYRRR
