ID   A0A0K1JZX5_9BURK        Unreviewed;       412 AA.
AC   A0A0K1JZX5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=ACZ75_15390 {ECO:0000313|EMBL:AKU22644.1};
OS   Massilia sp. NR 4-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU22644.1, ECO:0000313|Proteomes:UP000056897};
RN   [1] {ECO:0000313|EMBL:AKU22644.1, ECO:0000313|Proteomes:UP000056897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU22644.1,
RC   ECO:0000313|Proteomes:UP000056897};
RA   Sul W.J.;
RT   "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT   national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL   Submitted (JUN-2015) 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; CP012201; AKU22644.1; -; Genomic_DNA.
DR   RefSeq; WP_050409545.1; NZ_CP012201.1.
DR   AlphaFoldDB; A0A0K1JZX5; -.
DR   STRING; 1678028.ACZ75_15390; -.
DR   KEGG; mnr:ACZ75_15390; -.
DR   PATRIC; fig|1678028.3.peg.3116; -.
DR   OrthoDB; 9783686at2; -.
DR   Proteomes; UP000056897; Chromosome.
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:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR   CDD; cd14668; mlta_B; 1.
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   PIRSF; PIRSF019422; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000056897};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..412
FT                   /note="peptidoglycan lytic exotransglycosylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005461885"
FT   DOMAIN          154..310
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
FT   REGION          35..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..60
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  44533 MW;  52D35A06A9ACD4B1 CRC64;
     MLFARRSLLV SPAPVAATAL ALFLSACGTT PPPAQPVKPV PVQPATPPAQ PAPVQPAPAA
     PARPAKTEFV PVRFSSLPGW TRDDVRAAWP AFMSSCGVLA KQADWKEPCT IARGVNGNDE
     KAIRLFFESF LQPHQVVAAD GANSGLVTGY YEPLLQGSRK RGGPFQTPLY KAPDDLVTVE
     LASVYPQLKG MRLRGRLQGK KVVPYSTRAE IEKADFKGKE LMWVDDSVEA FFLQVQGSGR
     VQLGDTQETV RVAYADQNGH PYKSIGKYLV EKGELTADQA SAQGIKAWIA GHPTRQQELF
     NANPSYIFFR EEKLPDPKVG PKGSLGVPLT PQRSVAVDAA QLPLGAPLFI ATTQPNSEVP
     LQRLVMAQDT GGAIKGAIRV DYFFGFGPEA AENAGRMKQS GNVWVLLPRL QR
//