ID   MLTE_BUCBP              Reviewed;         212 AA.
AC   Q89AM2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=bbp_245;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016826; AAO26972.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q89AM2; -.
DR   SMR; Q89AM2; -.
DR   STRING; 224915.bbp_245; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; AAO26972; AAO26972; bbp_245.
DR   KEGG; bab:bbp_245; -.
DR   eggNOG; COG0741; Bacteria.
DR   HOGENOM; CLU_103257_0_0_6; -.
DR   OMA; EVYRYMG; -.
DR   OrthoDB; 1444566at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF01464; SLT; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Lyase; Reference proteome.
FT   CHAIN           1..212
FT                   /note="Membrane-bound lytic murein transglycosylase E"
FT                   /id="PRO_0000196571"
SQ   SEQUENCE   212 AA;  24494 MW;  4E92D851AC72C41B CRC64;
     MKKVILFTYV IIFLVFLSGY SVVTKNIVHN IKNNYKNNVC SMKVMHLWFK IINLFSKKYN
     VDKKLITAII CVESSGNTHA VSISKAIGLM QIKPFSAGRE VYRFRGLLNQ PSDVDLYDPK
     INIDIGTSYI NILRNKILSG IKNSEILLYA TIISYAHGAS KLLKSFSYNK TLAIKKINKM
     KIKEFLDYIH NKYSEKKAWD YLSKVMYVYH LV