ID A0A1V3RRN3_9BURK Unreviewed; 425 AA.
AC A0A1V3RRN3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=B0E41_23375 {ECO:0000313|EMBL:OOG79524.1};
OS Hydrogenophaga sp. A37.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1945864 {ECO:0000313|EMBL:OOG79524.1, ECO:0000313|Proteomes:UP000189189};
RN [1] {ECO:0000313|EMBL:OOG79524.1, ECO:0000313|Proteomes:UP000189189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A37 {ECO:0000313|EMBL:OOG79524.1,
RC ECO:0000313|Proteomes:UP000189189};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOG79524.1}.
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DR EMBL; MUNZ01000176; OOG79524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3RRN3; -.
DR STRING; 1945864.B0E41_23375; -.
DR Proteomes; UP000189189; 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:UP000189189}.
FT DOMAIN 184..323
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 425 AA; 46483 MW; 21734F2D1193BA6E CRC64;
MRSGRSAFFS SGSSPFFRPE NMVHHTMKIN NTSAASASSS NKVMGGFGRG VGWRWMAALI
VGSLAACSSV PPSGPGRAPA TSSADEVPLP PLIQRQGSRW LPVRWADLPG WGLDSLHEVW
GAWARGCERP APMHAALCAE MRPLTMAGTA EQQAWIENRF QPYRVVEPDG STPQGLITGY
YEPIMAASRQ STFIHRTPLY APPPGLAAGQ PWYSRQEIDT LPAAQAALKG RVIAWLADPI
DALILQIQGS GRLQFKEPDG SIRTVRVAYA AHNGHPYQSV GKWLLDQRAI REANWEGIKA
WAANNPGRLN EMLWSNPRTV FFKEVQLTEL DARFGPRGAQ GVPLTPGRSI AVDPLSIPYG
TPVWIASRGV FYNQQRLVMA QDTGGAIVGA VRADLFTGWG GWGDAPYQLA SRLKQPLQMW
ALWPR
//
