ID A0A0W0Z8J9_9GAMM Unreviewed; 400 AA.
AC A0A0W0Z8J9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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_1 {ECO:0000313|EMBL:KTD65440.1};
GN ORFNames=Lsha_0257 {ECO:0000313|EMBL:KTD65440.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD65440.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD65440.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD65440.1,
RC ECO:0000313|Proteomes:UP000054600};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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};
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:KTD65440.1}.
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DR EMBL; LNYW01000011; KTD65440.1; -; Genomic_DNA.
DR RefSeq; WP_018576281.1; NZ_LNYW01000011.1.
DR AlphaFoldDB; A0A0W0Z8J9; -.
DR STRING; 1122169.Lsha_0257; -.
DR PATRIC; fig|1122169.6.peg.284; -.
DR eggNOG; COG2821; Bacteria.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000054600; 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; 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 ECO:0000256|PIRNR:PIRNR019422};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR019422};
KW Reference proteome {ECO:0000313|Proteomes:UP000054600}.
FT DOMAIN 133..290
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 400 AA; 45090 MW; 1F504E8EE01FD97D CRC64;
MKTKLIALTL ALAFLAIGIS GWWFWPSKGP QPTFRQVAFK HLPGWETAEL RKSLRTFQTS
CRAFIKQDPE RVVGTEQIDL QAKDWQPACH AALKVHPVNQ HTAKQFFQEW FTPVEFYDKK
PVKGLFTGYY MPLLKGSYKK TAEFNVPLYE VPDDLVTIDL GLFVPHLKNR KLVGRIAAKK
VVPYYTREQI NKGAIKNNAK VLLWIHSPID RLFLEIQGSG IVEMEDGKRL FVGYDGQNGA
PYTAIAGVLI KKGIMTKHNA SMQAIKRYLE AHPKEMDKVI NQNKSFVFFR KLSMEAALGS
QGVALTPGYS MAIDKEWIPM GAPLWLSTTR PDSKNPDTNK PMQRLMIAQD TGGAIRGKVR
GDVFWGGGDK ATLIAGHMKN EGHYWLLLPS HAIPRLETKA
//