ID   EMTA_KLEP3              Reviewed;         203 AA.
AC   B5XQ85;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=KPK_1989;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI08685.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XQ85; -.
DR   SMR; B5XQ85; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; ACI08685; ACI08685; KPK_1989.
DR   KEGG; kpe:KPK_1989; -.
DR   HOGENOM; CLU_103257_0_0_6; -.
DR   OMA; EVYRYMG; -.
DR   OrthoDB; 1444566at2; -.
DR   Proteomes; UP000001734; 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_1000144957"
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;  22345 MW;  F9E68175D4AC6E26 CRC64;
     MKLRWLLILV VFLAGCSSKH DYTNPPWNPE VPVKRAMQWM PISEKAGAAW GVDPQLITAI
     IAIESGGNPA VVSKSGAVGL MQLKPSTSGR DVYRRMGWRG EPSVSELKNP ERNISMGAAY
     LSILENGPLA GIKDPQVMRY AVVVSYANGA GALLRTFSSD RQDAIDEIND LDADEFFEHV
     VKKHPAPQAP RYIWKLQKAL DAM