EMTA_ECO57
ID EMTA_ECO57 Reviewed; 203 AA.
AC Q8XDJ7; Q7AEW4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 117.
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=Z1956, ECs1687;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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=AAG56044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB35111.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG56044.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB35111.1; ALT_INIT; Genomic_DNA.
DR PIR; H85697; H85697.
DR PIR; H90839; H90839.
DR RefSeq; NP_309715.1; NC_002695.1.
DR RefSeq; WP_001295616.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XDJ7; -.
DR SMR; Q8XDJ7; -.
DR STRING; 155864.EDL933_1888; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; AAG56044; AAG56044; Z1956.
DR EnsemblBacteria; BAB35111; BAB35111; ECs_1687.
DR GeneID; 67417489; -.
DR GeneID; 913179; -.
DR KEGG; ece:Z1956; -.
DR KEGG; ecs:ECs_1687; -.
DR PATRIC; fig|386585.9.peg.1786; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_103257_0_0_6; -.
DR OMA; EVYRYMG; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; 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_0000312906"
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; A510C1522D8C03DC CRC64;
MKLRWFAFLI VLLAGCSSKH DYTNPPWNAK VPVQRAMQWM PISQKAGAAW GVDPQLITAI
IAIESGGNPN AVSKSNAIGL MQLKASTSGR DVYRRMGWSG EPTTSELKNP ERNISMGAAY
LNILETGPLA GIEDPKVLQY ALVVSYANGA GALLRTFSSD RKKAISKIND LDADEFLDHV
ARNHPAPQAP RYIYKLEQAL DAM
