EMTA_KLEP7
ID EMTA_KLEP7 Reviewed; 203 AA.
AC A6TAW0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 78.
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=KPN78578_22700; ORFNames=KPN_02305;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABR77731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000647; ABR77731.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002910846.1; NC_009648.1.
DR AlphaFoldDB; A6TAW0; -.
DR SMR; A6TAW0; -.
DR STRING; 272620.KPN_02305; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; ABR77731; ABR77731; KPN_02305.
DR KEGG; kpn:KPN_02305; -.
DR HOGENOM; CLU_103257_0_0_6; -.
DR OMA; EVYRYMG; -.
DR Proteomes; UP000000265; 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_0000312909"
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; 22358 MW; 0CE6817DFC0F473C CRC64;
MKLRWLLILV VFLAGCSSKH DYTNPPWNPE VPVKRAMQWM PISEKAGAAW GVDPQLITAI
IAIESGGNPA VVSKSGAVGL MQLKPSTSGR DVYRRMGWRG EPSVSELKNP ERNISMGAAY
LSILENGPLA GIKDPQVMRY AVVVSYANGA GALLRTFSSN RQDAIEEIND LDADEFFEHV
VKKHPAPQAP RYIWKLQKAL DAM