ID A0A5C1PXU4_9BURK Unreviewed; 457 AA.
AC A0A5C1PXU4;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
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=EWH46_00660 {ECO:0000313|EMBL:QEM99425.1};
OS Sphaerotilus sulfidivorans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Sphaerotilaceae; Sphaerotilus.
OX NCBI_TaxID=639200 {ECO:0000313|EMBL:QEM99425.1, ECO:0000313|Proteomes:UP000323522};
RN [1] {ECO:0000313|EMBL:QEM99425.1, ECO:0000313|Proteomes:UP000323522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D-507 {ECO:0000313|EMBL:QEM99425.1,
RC ECO:0000313|Proteomes:UP000323522};
RA Fomenkov A., Gridneva E., Smolyakov D., Dubinina G., Vincze T.,
RA Grabovich M., Roberts R.J.;
RT "Complete Genome Sequence and Methylome Analysis of Sphaerotilus natans
RT subsp. sulfidivorans D-507.";
RL Submitted (FEB-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; CP035708; QEM99425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C1PXU4; -.
DR KEGG; snn:EWH46_00660; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000323522; 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: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; 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; 2.
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}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 49279 MW; 50C735599B78BAB8 CRC64;
MPTSSSPAPS ASRISSVMSS SSFRSRSVGL CRATLRPRSG LSLAAALILG TLAGCGTPPR
PTDSAPPPLE IPPSVQTPPP LASDAEVRTT PRGRWVKAEW RDLPGWDQDT LTLAWPALTK
SCDKALTAAN GGNTSGRGLA AAAVATGTVG LSPFAVASAW NATCREVRRI GPTPTEAQVR
QLLQQRLQPW RIESAEGRTD GLLTGYFEPL LEASRTRTAR HTVPIHAMPA DLASRKPWYT
RGEIDSLPAA QAALKGREIA WLADPMDLLL VQIQGSGRLA FTAPDGQRSI TRLAFAGHND
QPYQSVGRWL VEQGAFTLEQ ASWPAIRQWA RQNPQRVKEM LAVNTRYVFF REEPLPDPSV
GAVGAQGVPL TPGRSIAVDK DSIPYGTPVW LASTEPQPWS ATPPAPRPLQ RLVVAQDTGS
AIIGAVRADY FWGWGDGAED RAGRTKQPLR LWALWPK
//
