ID   MLTE_BUCAI              Reviewed;         221 AA.
AC   P57352;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase E;
DE            EC=4.2.2.n1;
DE   AltName: Full=Murein hydrolase E;
GN   Name=mltE; OrderedLocusNames=BU264;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC         non-reducing ends of the peptidoglycan chains, with concomitant
CC         formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family. {ECO:0000305}.
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DR   EMBL; BA000003; BAB12974.1; -; Genomic_DNA.
DR   RefSeq; NP_240088.1; NC_002528.1.
DR   RefSeq; WP_010896032.1; NC_002528.1.
DR   AlphaFoldDB; P57352; -.
DR   SMR; P57352; -.
DR   STRING; 107806.10038939; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; BAB12974; BAB12974; BAB12974.
DR   KEGG; buc:BU264; -.
DR   PATRIC; fig|107806.10.peg.274; -.
DR   eggNOG; COG0741; Bacteria.
DR   HOGENOM; CLU_103257_0_0_6; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
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; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Lyase; Reference proteome.
FT   CHAIN           1..221
FT                   /note="Membrane-bound lytic murein transglycosylase E"
FT                   /id="PRO_0000196570"
SQ   SEQUENCE   221 AA;  25196 MW;  A3E7BF83D5700D71 CRC64;
     MFQSSIYNKN YKKFLKNLKY QGEYAVTLGI LAISILLLTG FNQFLNTKPT LKKNYFLNQK
     SIKNTLKNWN DIIATTANKY KVDEKLIKSI VYVESSGNPY AKSQSNAIGL MQIKPSSAGA
     EVYRLNGKKG RPSIQELYDP KTNIDIGTSY ISFLQKKFIS IKNKDVMRYA IIVAYVNGTS
     ALLKTFSKSR KEAINIINTM TKKSFCTHIK KNTRQCKHFV I