ID A0A1C3K5U5_9BURK Unreviewed; 421 AA.
AC A0A1C3K5U5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ODI_01001 {ECO:0000313|EMBL:SBT26876.1}, ODI_R4224
GN {ECO:0000313|EMBL:SOE52482.1};
OS Orrella dioscoreae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Orrella.
OX NCBI_TaxID=1851544 {ECO:0000313|EMBL:SBT26876.1, ECO:0000313|Proteomes:UP000078558};
RN [1] {ECO:0000313|EMBL:SBT26876.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SBT26876.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SOE52482.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SOE52482.1};
RA de Groot N.N.;
RL Submitted (AUG-2017) 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; FLRC01000044; SBT26876.1; -; Genomic_DNA.
DR EMBL; LT907988; SOE52482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C3K5U5; -.
DR STRING; 1851544.ODI_01001; -.
DR KEGG; odi:ODI_R4224; -.
DR Proteomes; UP000078558; Chromosome i.
DR Proteomes; UP000078558; 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 Glycosidase {ECO:0000313|EMBL:SBT26876.1};
KW Hydrolase {ECO:0000313|EMBL:SBT26876.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000078558}.
FT DOMAIN 155..314
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 44985 MW; A6E5F088D44DD8F7 CRC64;
MAGCASPPAP DDTAPSVPGM PGAKPLPAEG PLTVPPLSRL PDTTPRKLAG GFTQATWRDL
PGWDADNLEQ VWEGFLRNCR GLMRPTGGSL TAPARAAPRD WQPVCAIAAD PARAPAAGDT
AAVRQFLQTY LQPWRVLGAD GKPAANTVTG YYEPLVRGSR EQGGKYQWPL YAVPKDLLVI
DLGGLYPELA GKRVRGKLQG RRVVPYDTRE QINAGAEKPA VLAWIDDPVD AFFLQIQGSG
RVALTGGPGA GDTIRLAYAD HNGHPYGSVG KWLADKGELP LAQTSMQNIR LWAQRNPGRV
NEMLNVNPAM VFFSEEAITD PSAGPRGAYG VPLTEARSVA VDASFVPLGT PVFLATTRPA
SQTAMNRLVF AQDTGAAIKG AARTDFYWGY GDAAGEQAGR MKQRGQMWVL WPKAAGQPKA
R
//
