ID A0A0W0VAF1_9GAMM Unreviewed; 410 AA.
AC A0A0W0VAF1;
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 {ECO:0000313|EMBL:KTD17044.1};
GN ORFNames=Ljor_1350 {ECO:0000313|EMBL:KTD17044.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD17044.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD17044.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD17044.1,
RC ECO:0000313|Proteomes:UP000055035};
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:KTD17044.1}.
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DR EMBL; LNYJ01000011; KTD17044.1; -; Genomic_DNA.
DR RefSeq; WP_058470843.1; NZ_RDQQ01000007.1.
DR AlphaFoldDB; A0A0W0VAF1; -.
DR STRING; 456.Ljor_1350; -.
DR PATRIC; fig|456.5.peg.1444; -.
DR OrthoDB; 9783686at2; -.
DR Proteomes; UP000055035; 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:UP000055035}.
FT DOMAIN 133..290
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
SQ SEQUENCE 410 AA; 46149 MW; FF527567AB238AFC CRC64;
MKRTLLYSLL AISLLGAGFA VWWFWPNPPR PIALKQASFT SLPGWDKANV SKSLQTFQIS
CKTFLKQDPE KLVGSHHLNL KAKDWHPACQ AALAINSVTP ENAKAFFQKW FTPLEFYNGK
PVQGLFTGYY MPLLYGSRTK TDKFNVPIYG LPSDLLTIDL SQFDPNLKHK KLIGRVSGHR
VVPYYTRAQI NKGAIKKKAP VLVWIDNPVD RVFLEIQGSG IVELPDGQRI YLGYAAQNGA
PYTAIAKVLI DKGVMTKHNA SMQAIKRYLM SHPKEMNQVL NQNKSFVFFE ELRMNAALGT
QGVALTPGYS LAIDLKWIPM GTPLWLNTTR PDRQSDNQKP FQRLMIAQDT GGAIRGLVRG
DVFWGAGKKA TYIAGHMKNE GHYWLLLPHH ATERLQQEFA TLKDKIPLGK
//
