ID   EMTA_ECOLC              Reviewed;         203 AA.
AC   B1IU99;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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}; OrderedLocusNames=EcolC_2432;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000946; ACA78066.1; -; Genomic_DNA.
DR   RefSeq; WP_001301104.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IU99; -.
DR   SMR; B1IU99; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   KEGG; ecl:EcolC_2432; -.
DR   HOGENOM; CLU_103257_0_0_6; -.
DR   OMA; EVYRYMG; -.
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_1000087303"
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;  22227 MW;  A511D1432D8C03DC CRC64;
     MKLRWFAFLI VLLAGCSSKH DYTNPPWNAK VPVQRAMQWM PISQKAGAAW GVDPQLITAI
     IAIESGGNPN AVSKSNAIGL MQLKASTSGR DVYRRMGWSG EPTTSELKNP ERNISMGAAY
     LNILETGPLA GIEDPKVLQY ALVVSYANGA GALLRTFSSD RKKAISKIND LDADEFLEHV
     ARNHPAPQAP RYIYKLEQAL DAM