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Protein

Membrane-bound lytic murein transglycosylase A

Gene

mltA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi.

Catalytic activityi

Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.

pH dependencei

Optimum pH is 4.0-4.5.

Temperature dependencei

Loses rapidly its activity at temperatures above 30 degrees Celsius.

GO - Molecular functioni

  • carbon-oxygen lyase activity, acting on polysaccharides Source: UniProtKB-EC
  • hydrolase activity, hydrolyzing O-glycosyl compounds Source: EcoCyc
  • lytic transglycosylase activity Source: EcoliWiki

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan biosynthetic process Source: EcoCyc
  • peptidoglycan turnover Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciEcoCyc:G7457-MONOMER.
ECOL316407:JW2784-MONOMER.
MetaCyc:G7457-MONOMER.

Protein family/group databases

CAZyiGH102. Glycoside Hydrolase Family 102.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-bound lytic murein transglycosylase A (EC:4.2.2.n1)
Alternative name(s):
Mlt38
Murein hydrolase A
Gene namesi
Name:mltA
Synonyms:mlt, ygdM
Ordered Locus Names:b2813, JW2784
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13085. mltA.

Subcellular locationi

GO - Cellular componenti

  • cell outer membrane Source: UniProtKB-SubCell
  • cytosol Source: EcoCyc
  • integral component of membrane Source: EcoCyc
  • integral component of plasma membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020CuratedAdd
BLAST
Chaini21 – 365345Membrane-bound lytic murein transglycosylase APRO_0000032781Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi21 – 211N-palmitoyl cysteineCurated
Lipidationi21 – 211S-diacylglycerol cysteineCurated

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP0A935.
PRIDEiP0A935.

Interactioni

Subunit structurei

Forms a trimeric complex with MrcB/PonB and MipA in vitro.

Binary interactionsi

WithEntry#Exp.IntActNotes
proVP141751EBI-1130483,EBI-546797

Protein-protein interaction databases

BioGridi4261126. 187 interactions.
DIPiDIP-51238N.
IntActiP0A935. 1 interaction.
STRINGi511145.b2813.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 469Combined sources
Helixi56 – 6914Combined sources
Helixi71 – 8919Combined sources
Helixi94 – 1007Combined sources
Beta strandi102 – 1076Combined sources
Turni109 – 1124Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi125 – 1317Combined sources
Beta strandi138 – 1425Combined sources
Helixi148 – 1503Combined sources
Helixi153 – 1575Combined sources
Helixi163 – 1653Combined sources
Beta strandi166 – 1716Combined sources
Helixi173 – 18210Combined sources
Beta strandi185 – 1884Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi196 – 2038Combined sources
Helixi211 – 2177Combined sources
Helixi223 – 2253Combined sources
Helixi228 – 2369Combined sources
Helixi240 – 2478Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi276 – 2794Combined sources
Turni282 – 2843Combined sources
Beta strandi290 – 2989Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi304 – 31714Combined sources
Beta strandi327 – 3348Combined sources
Helixi335 – 3417Combined sources
Beta strandi346 – 35510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AE0X-ray2.00X22-365[»]
2GAEX-ray2.50A22-365[»]
2PI8X-ray2.25A/B/C/D22-365[»]
2PICX-ray2.25A22-365[»]
2PJJX-ray2.46A22-365[»]
ProteinModelPortaliP0A935.
SMRiP0A935. Positions 23-357.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A935.

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CA3. Bacteria.
COG2821. LUCA.
HOGENOMiHOG000278098.
InParanoidiP0A935.
KOiK08304.
OMAiKREDMSM.
OrthoDBiEOG6D2KR5.
PhylomeDBiP0A935.

Family and domain databases

Gene3Di2.40.40.10. 2 hits.
InterProiIPR010611. 3D_dom.
IPR005300. Lytic_transglycosylase_MltA.
IPR009009. RlpA-like_DPBB.
[Graphical view]
PfamiPF06725. 3D. 1 hit.
PF03562. MltA. 1 hit.
[Graphical view]
SMARTiSM00925. MltA. 1 hit.
[Graphical view]
SUPFAMiSSF50685. SSF50685. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A935-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGRWVKYLL MGTVVAMLAA CSSKPTDRGQ QYKDGKFTQP FSLVNQPDAV
60 70 80 90 100
GAPINAGDFA EQINHIRNSS PRLYGNQSNV YNAVQEWLRA GGDTRNMRQF
110 120 130 140 150
GIDAWQMEGA DNYGNVQFTG YYTPVIQARH TRQGEFQYPI YRMPPKRGRL
160 170 180 190 200
PSRAEIYAGA LSDKYILAYS NSLMDNFIMD VQGSGYIDFG DGSPLNFFSY
210 220 230 240 250
AGKNGHAYRS IGKVLIDRGE VKKEDMSMQA IRHWGETHSE AEVRELLEQN
260 270 280 290 300
PSFVFFKPQS FAPVKGASAV PLVGRASVAS DRSIIPPGTT LLAEVPLLDN
310 320 330 340 350
NGKFNGQYEL RLMVALDVGG AIKGQHFDIY QGIGPEAGHR AGWYNHYGRV
360
WVLKTAPGAG NVFSG
Length:365
Mass (Da):40,411
Last modified:July 19, 2005 - v1
Checksum:i5ECBB92C1E8D5969
GO

Sequence cautioni

The sequence AAB40463.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti346 – 3461H → N in AAC45723 (PubMed:9287002).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32224 Genomic DNA. Translation: AAC45723.1.
U29581 Genomic DNA. Translation: AAB40463.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75855.1.
AP009048 Genomic DNA. Translation: BAE76885.1.
PIRiA65064.
RefSeqiNP_417293.1. NC_000913.3.
WP_000678646.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75855; AAC75855; b2813.
BAE76885; BAE76885; BAE76885.
GeneIDi944964.
KEGGiecj:JW2784.
eco:b2813.
PATRICi32121044. VBIEscCol129921_2914.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32224 Genomic DNA. Translation: AAC45723.1.
U29581 Genomic DNA. Translation: AAB40463.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75855.1.
AP009048 Genomic DNA. Translation: BAE76885.1.
PIRiA65064.
RefSeqiNP_417293.1. NC_000913.3.
WP_000678646.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AE0X-ray2.00X22-365[»]
2GAEX-ray2.50A22-365[»]
2PI8X-ray2.25A/B/C/D22-365[»]
2PICX-ray2.25A22-365[»]
2PJJX-ray2.46A22-365[»]
ProteinModelPortaliP0A935.
SMRiP0A935. Positions 23-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261126. 187 interactions.
DIPiDIP-51238N.
IntActiP0A935. 1 interaction.
STRINGi511145.b2813.

Protein family/group databases

CAZyiGH102. Glycoside Hydrolase Family 102.

Proteomic databases

PaxDbiP0A935.
PRIDEiP0A935.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75855; AAC75855; b2813.
BAE76885; BAE76885; BAE76885.
GeneIDi944964.
KEGGiecj:JW2784.
eco:b2813.
PATRICi32121044. VBIEscCol129921_2914.

Organism-specific databases

EchoBASEiEB2894.
EcoGeneiEG13085. mltA.

Phylogenomic databases

eggNOGiENOG4105CA3. Bacteria.
COG2821. LUCA.
HOGENOMiHOG000278098.
InParanoidiP0A935.
KOiK08304.
OMAiKREDMSM.
OrthoDBiEOG6D2KR5.
PhylomeDBiP0A935.

Enzyme and pathway databases

BioCyciEcoCyc:G7457-MONOMER.
ECOL316407:JW2784-MONOMER.
MetaCyc:G7457-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A935.
PROiP0A935.

Family and domain databases

Gene3Di2.40.40.10. 2 hits.
InterProiIPR010611. 3D_dom.
IPR005300. Lytic_transglycosylase_MltA.
IPR009009. RlpA-like_DPBB.
[Graphical view]
PfamiPF06725. 3D. 1 hit.
PF03562. MltA. 1 hit.
[Graphical view]
SMARTiSM00925. MltA. 1 hit.
[Graphical view]
SUPFAMiSSF50685. SSF50685. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli."
    Lommatzsch J., Templin M.F., Kraft A.R., Vollmer W., Hoeltje J.-V.
    J. Bacteriol. 179:5465-5470(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli."
    Ursinus A., Hoeltje J.-V.
    J. Bacteriol. 176:338-343(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 147-161; 204-213 AND 258-280, CHARACTERIZATION.
  5. "Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli."
    Vollmer W., von Rechenberg M., Hoeltje J.-V.
    J. Biol. Chem. 274:6726-6734(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIPA AND MRCB/PONB.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

Entry informationi

Entry nameiMLTA_ECOLI
AccessioniPrimary (citable) accession number: P0A935
Secondary accession number(s): P46885
, P76638, Q2MA21, Q46928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 11, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.