ID D8MW96_ERWBE Unreviewed; 381 AA.
AC D8MW96;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Membrane-bound lytic murein transglycosylase A {ECO:0000256|PIRNR:PIRNR019422};
DE EC=4.2.2.n1 {ECO:0000256|PIRNR:PIRNR019422};
DE AltName: Full=Murein hydrolase A {ECO:0000256|PIRNR:PIRNR019422};
GN Name=mltA {ECO:0000313|EMBL:CAX61103.1};
GN OrderedLocusNames=EbC_35720 {ECO:0000313|EMBL:CAX61103.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|EMBL:CAX61103.1, ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX61103.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX61103.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC muropeptides during cell elongation and/or cell division.
CC {ECO:0000256|PIRNR:PIRNR019422}.
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 ECO:0000256|PIRNR:PIRNR019422};
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DR EMBL; FP236843; CAX61103.1; -; Genomic_DNA.
DR RefSeq; WP_013203587.1; NC_014306.1.
DR AlphaFoldDB; D8MW96; -.
DR STRING; 634500.EbC_35720; -.
DR CAZy; GH102; Glycoside Hydrolase Family 102.
DR KEGG; ebi:EbC_35720; -.
DR eggNOG; COG2821; Bacteria.
DR HOGENOM; CLU_037751_2_0_6; -.
DR Proteomes; UP000008793; 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:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR CDD; cd22785; DPBB_MltA-like; 1.
DR CDD; cd14472; mltA_B_like; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|PIRNR:PIRNR019422}; Glycosidase {ECO:0000313|EMBL:CAX61103.1};
KW Hydrolase {ECO:0000313|EMBL:CAX61103.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR019422};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..381
FT /note="Membrane-bound lytic murein transglycosylase A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003118298"
FT DOMAIN 125..259
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 381 AA; 41652 MW; 7BF9CA398F298A01 CRC64;
MKGCWAKFAV TGALLALLAG CSSKPTDRGQ QYKDGKLDEP LGLVNQPNAK GRPVNGKDFS
DQVSEIQYAS PAMYSRQTGT YGSIKAWLMA GGDTRQLRQF GLDAYQMEGT DNYGNVQFTG
YYTPVLQARY TRQGEFQYPL YRMPARAKGG RLPSRADIYS GALGDRYIVG YSNSLMDNFI
MDVQGSGYVD YGDGRPLTFF GYGGKNGHAY RSIGKVLIDR GEVKREDMSM QAIRKWGEEH
SPEQVRELLE QNPSFVFFKP ENFAPVRGAS AVPLVAKASV ASDRSLIPPG TALLAEVPIL
DNNGKFTGKY EMRMMVSLDV GGAIKGQHFD IYQGIGEQAG HMAGWFNHYG RVWVLKSAPG
AGVPVFSSAS NSTNGSALLT Q
//
