ID   EMTA_ECOK1              Reviewed;         203 AA.
AC   A1AAB6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Endo-type membrane-bound lytic murein transglycosylase A {ECO:0000255|HAMAP-Rule:MF_01381};
DE            EC=4.2.2.n2 {ECO:0000255|HAMAP-Rule:MF_01381};
DE   AltName: Full=Peptidoglycan lytic endotransglycosylase {ECO:0000255|HAMAP-Rule:MF_01381};
DE   Flags: Precursor;
GN   Name=emtA {ECO:0000255|HAMAP-Rule:MF_01381}; Synonyms=mltE;
GN   OrderedLocusNames=Ecok1_11120; ORFNames=APECO1_305;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; 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       Preferentially cleaves at a distance of more than two disaccharide
CC       units from the ends of the glycan chain. {ECO:0000255|HAMAP-
CC       Rule:MF_01381}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan with concomitant formation of a
CC         1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01381};
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01381}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01381}.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000255|HAMAP-Rule:MF_01381}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ00606.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000468; ABJ00606.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001295994.1; NC_008563.1.
DR   AlphaFoldDB; A1AAB6; -.
DR   SMR; A1AAB6; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; ABJ00606; ABJ00606; APECO1_305.
DR   KEGG; ecv:APECO1_305; -.
DR   HOGENOM; CLU_103257_0_0_6; -.
DR   Proteomes; UP000008216; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:UniProtKB-UniRule.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:InterPro.
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_01381; EmtA; 1.
DR   InterPro; IPR023946; EmtA.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_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..15
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01381"
FT   CHAIN           16..203
FT                   /note="Endo-type membrane-bound lytic murein
FT                   transglycosylase A"
FT                   /id="PRO_0000312907"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01381"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01381"
SQ   SEQUENCE   203 AA;  22213 MW;  A760C4522D8C06DC CRC64;
     MKLRWFAFLI VLLAGCSSKH DYTNPPWNAK VPVQRAMQWM PISQKAGAAW GVDPQLITAI
     IAIESGGNPN AVSKSNAIGL MQIKASTSGR DVYRRMGWSG EPTTSELKNP ERNISMGAAY
     LNILETGPLA GIEDPKVLQY ALVVSYANGA GALLRTFSSD RKKAISKIND LDADEFLDHV
     ARNHPAPQAP RYIYKLEQAL DAM