MLTA_ECOLI
ID MLTA_ECOLI Reviewed; 365 AA.
AC P0A935; P46885; P76638; Q2MA21; Q46928;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
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; Synonyms=mlt, ygdM; OrderedLocusNames=b2813, JW2784;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=9287002; DOI=10.1128/jb.179.17.5465-5470.1997;
RA Lommatzsch J., Templin M.F., Kraft A.R., Vollmer W., Hoeltje J.-V.;
RT "Outer membrane localization of murein hydrolases: MltA, a third
RT lipoprotein lytic transglycosylase in Escherichia coli.";
RL J. Bacteriol. 179:5465-5470(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 147-161; 204-213 AND 258-280, AND CHARACTERIZATION.
RX PubMed=8288527; DOI=10.1128/jb.176.2.338-343.1994;
RA Ursinus A., Hoeltje J.-V.;
RT "Purification and properties of a membrane-bound lytic transglycosylase
RT from Escherichia coli.";
RL J. Bacteriol. 176:338-343(1994).
RN [5]
RP INTERACTION WITH MIPA AND MRCB/PONB.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=10037771; DOI=10.1074/jbc.274.10.6726;
RA Vollmer W., von Rechenberg M., Hoeltje J.-V.;
RT "Demonstration of molecular interactions between the murein polymerase
RT PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of
RT Escherichia coli.";
RL J. Biol. Chem. 274:6726-6734(1999).
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.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0-4.5.;
CC Temperature dependence:
CC Loses rapidly its activity at temperatures above 30 degrees Celsius.;
CC -!- SUBUNIT: Forms a trimeric complex with MrcB/PonB and MipA in vitro.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40463.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U32224; AAC45723.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40463.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75855.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76885.1; -; Genomic_DNA.
DR PIR; A65064; A65064.
DR RefSeq; NP_417293.1; NC_000913.3.
DR RefSeq; WP_000678646.1; NZ_STEB01000030.1.
DR PDB; 2AE0; X-ray; 2.00 A; X=22-365.
DR PDB; 2GAE; X-ray; 2.50 A; A=22-365.
DR PDB; 2PI8; X-ray; 2.25 A; A/B/C/D=22-365.
DR PDB; 2PIC; X-ray; 2.25 A; A=22-365.
DR PDB; 2PJJ; X-ray; 2.46 A; A=22-365.
DR PDBsum; 2AE0; -.
DR PDBsum; 2GAE; -.
DR PDBsum; 2PI8; -.
DR PDBsum; 2PIC; -.
DR PDBsum; 2PJJ; -.
DR AlphaFoldDB; P0A935; -.
DR SMR; P0A935; -.
DR BioGRID; 4261126; 189.
DR DIP; DIP-51238N; -.
DR IntAct; P0A935; 2.
DR STRING; 511145.b2813; -.
DR CAZy; GH102; Glycoside Hydrolase Family 102.
DR jPOST; P0A935; -.
DR PaxDb; P0A935; -.
DR PRIDE; P0A935; -.
DR EnsemblBacteria; AAC75855; AAC75855; b2813.
DR EnsemblBacteria; BAE76885; BAE76885; BAE76885.
DR GeneID; 66673320; -.
DR GeneID; 944964; -.
DR KEGG; ecj:JW2784; -.
DR KEGG; eco:b2813; -.
DR PATRIC; fig|1411691.4.peg.3920; -.
DR EchoBASE; EB2894; -.
DR eggNOG; COG2821; Bacteria.
DR HOGENOM; CLU_037751_2_0_6; -.
DR InParanoid; P0A935; -.
DR OMA; DQNGHPY; -.
DR PhylomeDB; P0A935; -.
DR BioCyc; EcoCyc:G7457-MON; -.
DR BioCyc; MetaCyc:G7457-MON; -.
DR EvolutionaryTrace; P0A935; -.
DR PRO; PR:P0A935; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0036405; C:anchored component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0009279; C:cell outer membrane; IDA:CACAO.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; TAS:EcoCyc.
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:0008933; F:lytic transglycosylase activity; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Lipoprotein; Lyase; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000305"
FT CHAIN 21..365
FT /note="Membrane-bound lytic murein transglycosylase A"
FT /id="PRO_0000032781"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="H -> N (in Ref. 1; AAC45723)"
FT /evidence="ECO:0000305"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 71..89
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2AE0"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:2AE0"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2GAE"
FT STRAND 304..317
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:2AE0"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:2AE0"
FT STRAND 346..355
FT /evidence="ECO:0007829|PDB:2AE0"
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
