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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei309 – 3091UniRule 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

BioCyciILOI283942:MONOMERI0U-74.

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
Ordered Locus Names:IL0587
OrganismiIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Taxonomic identifieri283942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina
Proteomesi
  • UP000001171 Componenti: Chromosome

Subcellular locationi

  • Cell outer membrane; Peripheral membrane protein

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

GO - Cellular componenti

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 – 455434Membrane-bound lytic murein transglycosylase FPRO_0000353946Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi283942.IL0587.

Structurei

3D structure databases

ProteinModelPortaliQ5QWY4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 264243Non-LT domainUniRule annotationAdd
BLAST
Regioni265 – 455191LT domainUniRule annotationAdd
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.UniRule annotation

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.
KOiK18691.
OMAiYYDILTW.
OrthoDBiEOG62C9FB.

Family and domain databases

HAMAPiMF_02016. MltF.
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. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5QWY4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKSAVSLFA ILLLAASVIT ACSPQTRPDA MSVVQERQVL RVGTLINPTS
60 70 80 90 100
YYFDHDREQG FEYDLAKRFA DRLGVELEMV PRFDVNDLFT MLRRGEVDIV
110 120 130 140 150
AAGLDRTSTR AQLFRFSPPY DIISQKVVFK QGSRQRPRDL QQITDGEIVV
160 170 180 190 200
VEGSSHHEFL KSLGDSIPTL KWRATRDHDA VELLQMVISG EVDYTITDST
210 220 230 240 250
ALDIQRRFHP DLSVAFTVKH DQDIAWALPQ GKDDSLFAAV IEYFGEIRSS
260 270 280 290 300
GRLAHIKEQH FGHVKQFNYV TTSLFIEAVE QVLPGYIETF KEHSGSLDWR
310 320 330 340 350
LLAAISYQES LWNPRAVSPT GVRGMMMLTL PTAKAMGVKS RLNAEQSIRG
360 370 380 390 400
GARYLERMLN RVPARIPQPD RTWFAIAAYN IGFGHLEDAR IITERQGGNP
410 420 430 440 450
DRWVDVKKRL PLLRQKQFYR HTRYGFARGD EPVTYVGNIR RFYDTLKYLD

EQGRL
Length:455
Mass (Da):51,970
Last modified:January 4, 2005 - v1
Checksum:i45E825A30E64EDA0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017340 Genomic DNA. Translation: AAV81428.1.
RefSeqiWP_011233844.1. NC_006512.1.

Genome annotation databases

EnsemblBacteriaiAAV81428; AAV81428; IL0587.
KEGGiilo:IL0587.
PATRICi22139195. VBIIdiLoi21852_0589.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017340 Genomic DNA. Translation: AAV81428.1.
RefSeqiWP_011233844.1. NC_006512.1.

3D structure databases

ProteinModelPortaliQ5QWY4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi283942.IL0587.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV81428; AAV81428; IL0587.
KEGGiilo:IL0587.
PATRICi22139195. VBIIdiLoi21852_0589.

Phylogenomic databases

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
KOiK18691.
OMAiYYDILTW.
OrthoDBiEOG62C9FB.

Enzyme and pathway databases

BioCyciILOI283942:MONOMERI0U-74.

Family and domain databases

HAMAPiMF_02016. MltF.
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. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Entry informationi

Entry nameiMLTF_IDILO
AccessioniPrimary (citable) accession number: Q5QWY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: January 4, 2005
Last modified: June 8, 2016
This is version 69 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

Complete proteome, Reference proteome

Documents

  1. 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.