ID   MLTA_ECO57              Reviewed;         365 AA.
AC   P0A936; P46885; P76638; Q46928;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase A;
DE            EC=4.2.2.n1;
DE   AltName: Full=Mlt38;
DE   AltName: Full=Murein hydrolase A;
DE   Flags: Precursor;
GN   Name=mltA; OrderedLocusNames=Z4130, ECs3673;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division. Degrades
CC       murein glycan strands and insoluble, high-molecular weight murein
CC       sacculi (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR   EMBL; AE005174; AAG57927.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37096.1; -; Genomic_DNA.
DR   PIR; A98088; A98088.
DR   PIR; C85933; C85933.
DR   RefSeq; NP_311700.1; NC_002695.1.
DR   RefSeq; WP_000678646.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A936; -.
DR   SMR; P0A936; -.
DR   STRING; 155864.EDL933_3994; -.
DR   EnsemblBacteria; AAG57927; AAG57927; Z4130.
DR   EnsemblBacteria; BAB37096; BAB37096; ECs_3673.
DR   GeneID; 66673320; -.
DR   GeneID; 916516; -.
DR   KEGG; ece:Z4130; -.
DR   KEGG; ecs:ECs_3673; -.
DR   PATRIC; fig|386585.9.peg.3840; -.
DR   eggNOG; COG2821; Bacteria.
DR   HOGENOM; CLU_037751_2_0_6; -.
DR   OMA; DQNGHPY; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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; cd14485; mltA_like_LT_A; 1.
DR   Gene3D; 2.40.40.10; -; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR034654; MltA_3D.
DR   InterPro; IPR005300; MltA_B.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; PTHR30124; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03562; MltA; 1.
DR   PIRSF; PIRSF019422; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell wall biogenesis/degradation; Lipoprotein; Lyase;
KW   Membrane; Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..365
FT                   /note="Membrane-bound lytic murein transglycosylase A"
FT                   /id="PRO_0000032782"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   365 AA;  40411 MW;  5ECBB92C1E8D5969 CRC64;
     MKGRWVKYLL MGTVVAMLAA CSSKPTDRGQ QYKDGKFTQP FSLVNQPDAV GAPINAGDFA
     EQINHIRNSS PRLYGNQSNV YNAVQEWLRA GGDTRNMRQF GIDAWQMEGA DNYGNVQFTG
     YYTPVIQARH TRQGEFQYPI YRMPPKRGRL PSRAEIYAGA LSDKYILAYS NSLMDNFIMD
     VQGSGYIDFG DGSPLNFFSY AGKNGHAYRS IGKVLIDRGE VKKEDMSMQA IRHWGETHSE
     AEVRELLEQN PSFVFFKPQS FAPVKGASAV PLVGRASVAS DRSIIPPGTT LLAEVPLLDN
     NGKFNGQYEL RLMVALDVGG AIKGQHFDIY QGIGPEAGHR AGWYNHYGRV WVLKTAPGAG
     NVFSG