ID A0A263HCL0_9PAST Unreviewed; 365 AA.
AC A0A263HCL0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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:SUU35158.1};
GN ORFNames=NCTC10851_00752 {ECO:0000313|EMBL:SUU35158.1};
OS Actinobacillus seminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=722 {ECO:0000313|EMBL:SUU35158.1, ECO:0000313|Proteomes:UP000254507};
RN [1] {ECO:0000313|EMBL:SUU35158.1, ECO:0000313|Proteomes:UP000254507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10851 {ECO:0000313|EMBL:SUU35158.1,
RC ECO:0000313|Proteomes:UP000254507};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; UFSB01000001; SUU35158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263HCL0; -.
DR InParanoid; A0A263HCL0; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000254507; 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-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
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; 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 ECO:0000256|PIRNR:PIRNR019422};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR019422}.
FT DOMAIN 139..268
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 365 AA; 40437 MW; F808B1F7BE4D5076 CRC64;
MWLKPLSIRK IAVIFGILFL PGCSSTQHTG NHSTQETNEK FGAQYVGRSY QQVNLMPVLE
VENKSAVRNQ GDFLTQLSNI YSYSQSLSKR FANVYRKITD WVLTGADIND LSTFDIHPQI
MKGQDGYQNV LMTGYYSPVI HARQTQQGKY NQPIYAMPTQ KRFTRAQIYA GALKGKGLEL
AYSDSMIDNF LLGVQGSGYV DFGNGDLNYF AYAGQNGFDY VAVGRLLVED GEIPKEKMSI
QAIKDWANAN PSRLQSLLER NPSYVFFKND PNGKVRGSAG VPLVPMASIA ADRSLIPSGS
VLLVEVPEID NEGNWIGKHK LNLMVALDVG GAVKGHHFDL YRGIGDEAGH IAGLSKHYGR
AWLLQ
//
