ID   A0A1I0RQ90_9RHOB        Unreviewed;       344 AA.
AC   A0A1I0RQ90;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SAMN04488515_3053 {ECO:0000313|EMBL:SEW43257.1};
OS   Cognatiyoonia koreensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cognatiyoonia.
OX   NCBI_TaxID=364200 {ECO:0000313|EMBL:SEW43257.1, ECO:0000313|Proteomes:UP000199167};
RN   [1] {ECO:0000313|EMBL:SEW43257.1, ECO:0000313|Proteomes:UP000199167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17925 {ECO:0000313|EMBL:SEW43257.1,
RC   ECO:0000313|Proteomes:UP000199167};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOIZ01000002; SEW43257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0RQ90; -.
DR   STRING; 364200.SAMN04488515_3053; -.
DR   Proteomes; UP000199167; 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; 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.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199167};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..344
FT                   /note="peptidoglycan lytic exotransglycosylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011503661"
FT   DOMAIN          101..236
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   344 AA;  37897 MW;  D44E846E8A8C908E CRC64;
     MIQESAGPLC LALLLSGPVM AETTYTLLDY ADLNGWAQDD HDAALSVFAQ TCGDIPRYEF
     ERLCAFAKDA PPARDFFETF FQPVLIEDGD PMLFTGYYEP EISGSLAPTD EFRFPLYRVP
     PDLVEGQTYL SRREIDESDA LKDKALEIAW LSDPVDLFFL QVQGSGRIKL PDGGVIRVGY
     GGKNGRDYSS LGQTLVSRGV YQPHQVSAEV IRNWVRDNPD EGQELLWTNE SYVFFREVSE
     VPAELGPLGA MNRSITAMRS IAVDPSITLL GAPVWIEKEG ESPLNRLMIA QDTGSAIKGA
     QRADIFYGTG TKAGLEAGQI KDGGRMVVLM PVDYALAKTE QGFE
//