ID A0A069ICU5_9BURK Unreviewed; 389 AA.
AC A0A069ICU5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, 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=CF70_020095 {ECO:0000313|EMBL:KDP84331.1};
OS Cupriavidus sp. SK-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP84331.1, ECO:0000313|Proteomes:UP000023560};
RN [1] {ECO:0000313|EMBL:KDP84331.1, ECO:0000313|Proteomes:UP000023560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-3 {ECO:0000313|EMBL:KDP84331.1,
RC ECO:0000313|Proteomes:UP000023560};
RA Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT "Cupriavidus sp. strain SK-3.";
RL Submitted (MAY-2014) 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:KDP84331.1}.
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DR EMBL; JFJV02000260; KDP84331.1; -; Genomic_DNA.
DR RefSeq; WP_035872647.1; NZ_JFJV02000260.1.
DR AlphaFoldDB; A0A069ICU5; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000023560; 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; 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; 2.
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 DOMAIN 159..291
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 389 AA; 42076 MW; 583815F2D972959E CRC64;
MAYLHSFFRF PFSTPRGSAA QARKEAGGRR LGWLGLAAAA TLLAGCMSGP PPRVEGPGTR
PVTPPTGSAQ KGVLQAASWS EIGGWGQDDV RAAWPALQAS CQALKKRAEW NRVCALGMLV
DAGDLGAMRA YFESNFQPFR VVNSDGTDSG LITGYYEPIL HGARTRQGQY QVPLYRKPPQ
WGNRALPARA ELLQNPALRG QELVWVDDPV EAAFLQIQGS GRIRLQDGSV MRVGFGGTND
QPFRSFGKWL LDRGEITPAQ ATMQGIKAWA RANPGRVEEM LNINPRFVFF RELPSNNDGP
VGALGVPLTA ERSIAVDPAT IPLGVPVFLS TTRPLSTEPI QRLMFAQDTG TAIKGGVRAD
FFWGAGDAAG ETAGRMKQGG RMWVLMPRS
//
