EMTA_ECOLI
ID EMTA_ECOLI Reviewed; 203 AA.
AC P0C960; O87500; P76009; P94775;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 92.
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, sltZ, ycgP;
GN OrderedLocusNames=b1193, JW5821;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP IDENTIFICATION, PALMITOYLATION AT CYS-16, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION AS AN ENDO-TYPE TRANSGLYCOSYLASE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=9642199; DOI=10.1128/jb.180.13.3441-3447.1998;
RA Kraft A.R., Templin M.F., Hoeltje J.V.;
RT "Membrane-bound lytic endotransglycosylase in Escherichia coli.";
RL J. Bacteriol. 180:3441-3447(1998).
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. Prefers cross-linked murein in
CC vivo.
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:0000305|PubMed:9642199};
CC Lipid-anchor {ECO:0000305|PubMed:9642199}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000255|HAMAP-Rule:MF_01381}.
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DR EMBL; U00096; AAC74277.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA36051.2; -; Genomic_DNA.
DR PIR; F64865; F64865.
DR RefSeq; NP_415711.2; NC_000913.3.
DR RefSeq; WP_001301104.1; NZ_SSZK01000010.1.
DR PDB; 2Y8P; X-ray; 2.00 A; A/B=19-203.
DR PDB; 3T36; X-ray; 2.25 A; A/B/C/D/E=17-203.
DR PDB; 4HJV; X-ray; 2.30 A; A/B/C/D/E=17-203.
DR PDB; 4HJY; X-ray; 2.40 A; A/B=17-203.
DR PDB; 4HJZ; X-ray; 1.90 A; A/B=17-203.
DR PDB; 6GHY; X-ray; 2.12 A; A/B=19-203.
DR PDB; 6GHZ; X-ray; 2.33 A; A/B=19-203.
DR PDB; 6GI3; X-ray; 1.38 A; B=19-203.
DR PDB; 6GI4; X-ray; 1.35 A; B=19-203.
DR PDBsum; 2Y8P; -.
DR PDBsum; 3T36; -.
DR PDBsum; 4HJV; -.
DR PDBsum; 4HJY; -.
DR PDBsum; 4HJZ; -.
DR PDBsum; 6GHY; -.
DR PDBsum; 6GHZ; -.
DR PDBsum; 6GI3; -.
DR PDBsum; 6GI4; -.
DR AlphaFoldDB; P0C960; -.
DR SMR; P0C960; -.
DR BioGRID; 4259642; 360.
DR BioGRID; 850027; 2.
DR IntAct; P0C960; 2.
DR STRING; 511145.b1193; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR PaxDb; P0C960; -.
DR PRIDE; P0C960; -.
DR EnsemblBacteria; AAC74277; AAC74277; b1193.
DR EnsemblBacteria; BAA36051; BAA36051; BAA36051.
DR GeneID; 945655; -.
DR KEGG; ecj:JW5821; -.
DR KEGG; eco:b1193; -.
DR PATRIC; fig|1411691.4.peg.1093; -.
DR EchoBASE; EB3656; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_103257_0_0_6; -.
DR OMA; EVYRYMG; -.
DR PhylomeDB; P0C960; -.
DR BioCyc; EcoCyc:G6622-MON; -.
DR BioCyc; MetaCyc:G6622-MON; -.
DR BRENDA; 4.2.2.B6; 2026.
DR PRO; PR:P0C960; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; ISM:EcoCyc.
DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:UniProtKB-UniRule.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IDA:EcoCyc.
DR GO; GO:0008933; F:lytic transglycosylase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell wall biogenesis/degradation;
KW Lipoprotein; Lyase; 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_0000196568"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:9642199"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01381"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:6GI4"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:6GI4"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6GI4"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:6GI4"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:6GI4"
FT TURN 127..131
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:6GI4"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:6GI4"
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
