ID E1TA49_BURSG Unreviewed; 374 AA.
AC E1TA49;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 OrderedLocusNames=BC1003_3077 {ECO:0000313|EMBL:ADN59026.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN59026.1};
RN [1] {ECO:0000313|EMBL:ADN59026.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN59026.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) 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; CP002217; ADN59026.1; -; Genomic_DNA.
DR AlphaFoldDB; E1TA49; -.
DR STRING; 640512.BC1003_3077; -.
DR CAZy; GH102; Glycoside Hydrolase Family 102.
DR KEGG; bgf:BC1003_3077; -.
DR eggNOG; COG2821; Bacteria.
DR HOGENOM; CLU_037751_0_0_4; -.
DR OrthoDB; 9783686at2; -.
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; 2.40.40.10; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT DOMAIN 136..269
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 374 AA; 40015 MW; B7D8BE394EEED5A4 CRC64;
MRFVRATGAW LGALSVAAIL AACGGGGAVR PVSSPPTGAA VIPGQIAATR LTAVAWQQVP
GWQDDSLIGA TAALRQNCVR LARQPNWARA CAAAAQLDDL DSTSARAFFE AYFTPFQLAN
NDGTLDGLVT GYYEPLLRGS RTRHGVYQTA LYRWPSSYRP GAPMPPRAQL ERMGVLNGNE
LVWVDDPIEA FFLQVQGSGR IVMEDGSVMR VGFGGTNNQP YKSIGRWLLD RGELTPAQAT
MQGIKAWARA NPNRVDALLD TNPRFVFFRE MPSAEAMPKG GADGPIGALG VPLTPERSIA
VDPASIPLGT PVFLQTTRPL TNSPMNRLVF AQDTGSAIKG GVRADYFWGL GDDAGDLAGK
MKQGGRMWLL LPNS
//
