ID MLTC_ECOK1 Reviewed; 359 AA.
AC A1AFE9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 27-MAR-2024, entry version 95.
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=Ecok1_28950;
GN ORFNames=APECO1_3538;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
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=ABJ02389.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000468; ABJ02389.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000760323.1; NZ_CADILS010000010.1.
DR AlphaFoldDB; A1AFE9; -.
DR SMR; A1AFE9; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR GeneID; 83579530; -.
DR KEGG; ecv:APECO1_3538; -.
DR HOGENOM; CLU_044583_0_0_6; -.
DR Proteomes; UP000008216; 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: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 CDD; cd16893; LT_MltC_MltE; 1.
DR Gene3D; 1.10.530.10; -; 1.
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 PANTHER; PTHR37423:SF3; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE C; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR Pfam; PF11873; Mltc_N; 1.
DR Pfam; PF01464; SLT; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 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_0000335582"
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; 40113 MW; 618F0FCC9C41969C CRC64;
MKKYLALALI APLLISCSTT KKGDTYNEAW 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
//
