ID   D0YW57_PHODD            Unreviewed;       302 AA.
AC   D0YW57;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=VDA_001339 {ECO:0000313|EMBL:EEZ40314.1};
OS   Photobacterium damselae subsp. damselae CIP 102761.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ40314.1, ECO:0000313|Proteomes:UP000003579};
RN   [1] {ECO:0000313|EMBL:EEZ40314.1, ECO:0000313|Proteomes:UP000003579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ40314.1,
RC   ECO:0000313|Proteomes:UP000003579};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA   Bartels D.;
RL   Submitted (NOV-2009) 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; ADBS01000001; EEZ40314.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0YW57; -.
DR   eggNOG; COG2821; Bacteria.
DR   Proteomes; UP000003579; Unassembled WGS sequence.
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; cd22785; DPBB_MltA-like; 1.
DR   CDD; cd14668; mlta_B; 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; 2.
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:UP000003579}.
FT   DOMAIN          53..186
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   302 AA;  33848 MW;  4AFF1C81F4C28910 CRC64;
     MDRKYGPLYR QLEKWIKTDG KVQDLTKYGI QAAQLGGSDD RGNVMFTGYY SPVLEIRHYP
     DAEYKYPVYA MPKCKGRCPS RAQIYAGALK GQGLELGYSK SMIDVFMMEV QGSGFVHYGD
     NDEMQYFGYA GKNGHRYVSI GKVLIDRGEV PRDKMSLKAI HDWAEKQSPA KLRELLEQNP
     SYVFFERRPS LDVKGSAGIP LLADSAVAGD RKYFPMGSVI LAEVPKLNEA GHWTGKHQLQ
     LFIVLDTGGA VKRNHFDIYH GRGEKAGIAA GHYKHFGRVW KLGLKGTATQ DPWLMANGQL
     SD
//