ID   A0A4U8YX58_METTU        Unreviewed;       189 AA.
AC   A0A4U8YX58;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-JUN-2025, entry version 15.
DE   RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE            EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
DE   AltName: Full=Murein hydrolase A {ECO:0000256|ARBA:ARBA00030918};
GN   ORFNames=MTUNDRAET4_0667 {ECO:0000313|EMBL:VFU07560.1};
OS   Methylocella tundrae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=227605 {ECO:0000313|EMBL:VFU07560.1, ECO:0000313|Proteomes:UP000294360};
RN   [1] {ECO:0000313|EMBL:VFU07560.1, ECO:0000313|Proteomes:UP000294360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTUNDRAET4 annotated genome {ECO:0000313|EMBL:VFU07560.1};
RA   Kox A.R. M.;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001420};
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DR   EMBL; LR536450; VFU07560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U8YX58; -.
DR   KEGG; mtun:MTUNDRAET4_0667; -.
DR   Proteomes; UP000294360; Chromosome 1.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008933; F:peptidoglycan lytic transglycosylase activity; IEA:TreeGrafter.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:TreeGrafter.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR   CDD; cd14485; mltA_like_LT_A; 1.
DR   Gene3D; 2.40.240.50; Barwin-like endoglucanases; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR005300; MltA_B.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   PANTHER; PTHR30124:SF0; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03562; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000294360}.
FT   DOMAIN          1..82
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   189 AA;  20399 MW;  0BDA7E68E462AF42 CRC64;
     MIQVQGSARV RLEDGRSLRL VYAGRNGWPY TSIGRILIDT REIAQDSMSL AALKQWIRAH
     GQRPGEEGAE LMRRNQSYVF FALAPDLDAE AGPIGGAGLS LTPLRSLAID RDIYPYGAPI
     WVDADIPGAL PEGRLRRLMI AQDTGSAIVG PARADIFFGS GDEAGARAGA VRHAGEFIVF
     LPVEEGSLR
//