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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

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

Functioni

Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.

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.UniRule annotation

pH dependencei

Optimum pH is 6.5-7.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei314 – 3141UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciEcoCyc:EG11373-MONOMER.
ECOL316407:JW2542-MONOMER.
MetaCyc:EG11373-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-bound lytic murein transglycosylase FUniRule annotation (EC:4.2.2.n1UniRule annotation)
Alternative name(s):
Murein lyase FUniRule annotation
Gene namesi
Name:mltFUniRule annotation
Synonyms:yfhD
Ordered Locus Names:b2558, JW2542
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11373. yfhD.

Subcellular locationi

  • Cell outer membrane UniRule annotation1 Publication; Peripheral membrane protein UniRule annotation1 Publication

  • Note: Attached to the inner leaflet of the outer membrane.

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121UniRule annotationAdd
BLAST
Chaini22 – 518497Membrane-bound lytic murein transglycosylase FPRO_0000196562Add
BLAST

Proteomic databases

PaxDbiP0AGC5.

Interactioni

Protein-protein interaction databases

BioGridi4259207. 7 interactions.
STRINGi511145.b2558.

Structurei

3D structure databases

ProteinModelPortaliP0AGC5.
SMRiP0AGC5. Positions 39-447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 269248Non-LT domainAdd
BLAST
Regioni270 – 518249LT domainAdd
BLAST

Domaini

The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain.

Sequence similaritiesi

In the N-terminal section; belongs to the bacterial solute-binding protein 3 family.UniRule annotation
In the C-terminal section; belongs to the transglycosylase Slt family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
InParanoidiP0AGC5.
KOiK18691.
OMAiKYGYARG.
PhylomeDBiP0AGC5.

Family and domain databases

HAMAPiMF_02016. MltF. 1 hit.
InterProiIPR023346. Lysozyme-like_dom.
IPR023703. MltF.
IPR001638. Solute-binding_3/MltF_N.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[Graphical view]
PANTHERiPTHR21666:SF215. PTHR21666:SF215. 1 hit.
PfamiPF00497. SBP_bac_3. 1 hit.
PF01464. SLT. 1 hit.
[Graphical view]
SMARTiSM00062. PBPb. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 2 hits.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0AGC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLKINYLF IGILALLLAV ALWPSIPWFG KADNRIAAIQ ARGELRVSTI
60 70 80 90 100
HTPLTYNEIN GKPFGLDYEL AKQFADYLGV KLKVTVRQNI SQLFDDLDNG
110 120 130 140 150
NADLLAAGLV YNSERVKNYQ PGPTYYSVSQ QLVYKVGQYR PRTLGNLTAE
160 170 180 190 200
QLTVAPGHVV VNDLQTLKET KFPELSWKVD DKKGSAELME DVIEGKLDYT
210 220 230 240 250
IADSVAISLF QRVHPELAVA LDITDEQPVT WFSPLDGDNT LSAALLDFFN
260 270 280 290 300
EMNEDGTLAR IEEKYLGHGD DFDYVDTRTF LRAVDAVLPQ LKPLFEKYAE
310 320 330 340 350
EIDWRLLAAI AYQESHWDAQ ATSPTGVRGM MMLTKNTAQS LGITDRTDAE
360 370 380 390 400
QSISGGVRYL QDMMSKVPES VPENERIWFA LAAYNMGYAH MLDARALTAK
410 420 430 440 450
TKGNPDSWAD VKQRLPLLSQ KPYYSKLTYG YARGHEAYAY VENIRKYQIS
460 470 480 490 500
LVGYLQEKEK QATEAAMQLA QDYPAVSPTE LGKEKFPFLS FLSQSSSNYL
510
THSPSLLFSR KGSEEKQN
Length:518
Mass (Da):58,302
Last modified:May 20, 2008 - v2
Checksum:i70A5ABE842E47D4A
GO

Sequence cautioni

The sequence AAA79820 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA10908 differs from that shown. Reason: Frameshift at position 478. Curated
The sequence BAA10908 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE76734 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA51065 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1512EQ → DR in BAA10908 (Ref. 1) Curated
Sequence conflicti150 – 1512EQ → DR in M19501 (PubMed:2659070).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64044 Genomic DNA. Translation: BAA10908.1. Sequence problems.
U36841 Genomic DNA. Translation: AAA79820.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75611.2.
AP009048 Genomic DNA. Translation: BAE76734.1. Different initiation.
M19501 Genomic DNA. No translation available.
X72336 Genomic DNA. Translation: CAA51065.1. Frameshift.
PIRiE65033.
RefSeqiNP_417053.2. NC_000913.3.
WP_000734212.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75611; AAC75611; b2558.
BAE76734; BAE76734; BAE76734.
GeneIDi947028.
KEGGiecj:JW2542.
eco:b2558.
PATRICi32120515. VBIEscCol129921_2660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64044 Genomic DNA. Translation: BAA10908.1. Sequence problems.
U36841 Genomic DNA. Translation: AAA79820.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75611.2.
AP009048 Genomic DNA. Translation: BAE76734.1. Different initiation.
M19501 Genomic DNA. No translation available.
X72336 Genomic DNA. Translation: CAA51065.1. Frameshift.
PIRiE65033.
RefSeqiNP_417053.2. NC_000913.3.
WP_000734212.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AGC5.
SMRiP0AGC5. Positions 39-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259207. 7 interactions.
STRINGi511145.b2558.

Proteomic databases

PaxDbiP0AGC5.

Protocols and materials databases

DNASUi947028.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75611; AAC75611; b2558.
BAE76734; BAE76734; BAE76734.
GeneIDi947028.
KEGGiecj:JW2542.
eco:b2558.
PATRICi32120515. VBIEscCol129921_2660.

Organism-specific databases

EchoBASEiEB1347.
EcoGeneiEG11373. yfhD.

Phylogenomic databases

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
InParanoidiP0AGC5.
KOiK18691.
OMAiKYGYARG.
PhylomeDBiP0AGC5.

Enzyme and pathway databases

BioCyciEcoCyc:EG11373-MONOMER.
ECOL316407:JW2542-MONOMER.
MetaCyc:EG11373-MONOMER.

Miscellaneous databases

PROiP0AGC5.

Family and domain databases

HAMAPiMF_02016. MltF. 1 hit.
InterProiIPR023346. Lysozyme-like_dom.
IPR023703. MltF.
IPR001638. Solute-binding_3/MltF_N.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[Graphical view]
PANTHERiPTHR21666:SF215. PTHR21666:SF215. 1 hit.
PfamiPF00497. SBP_bac_3. 1 hit.
PF01464. SLT. 1 hit.
[Graphical view]
SMARTiSM00062. PBPb. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 2 hits.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMLTF_ECOLI
AccessioniPrimary (citable) accession number: P0AGC5
Secondary accession number(s): P30135, Q2MAH2, Q83QJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: May 20, 2008
Last modified: September 7, 2016
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

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.