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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Pseudomonas mendocina (strain ymp)
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)DescriptionActionsGraphical viewLength
Active sitei316UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cell wall biogenesis/degradation

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

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:Pmen_3415
OrganismiPseudomonas mendocina (strain ymp)
Taxonomic identifieri399739 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000000229 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25UniRule annotationAdd BLAST25
ChainiPRO_500024081526 – 488Membrane-bound lytic murein transglycosylase FAdd BLAST463

Structurei

3D structure databases

ProteinModelPortaliA4XXV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 269Non-LT domainUniRule annotationAdd BLAST244
Regioni270 – 488LT domainUniRule annotationAdd BLAST219

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.
OMAiKYGYARG.
OrthoDBiPOG091H03Q9.

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.
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.

A4XXV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFARPAIRMR CATGLLAIGT LLMLAGCGEE PKPSVLEQVK AEGELRVVTR
60 70 80 90 100
NSPATYFQDR NGATGFEYEL AKRFATDLGL ELKIETADNL DSLFASLGHV
110 120 130 140 150
DGPVLAAAGL VETPQRQRQA RFSVPYLEVT PQIIYRQGET RPTKAEDLLG
160 170 180 190 200
KRILVLAGSS HAEQLEALKL ELPELTFEVS DAVEVVDLLR MVDEGQIDLT
210 220 230 240 250
LVDSNELAMN QVYFPNVRVA FDLGDTNTMR WAVAPGEDDS LLLEIDAFLE
260 270 280 290 300
RSQANGTLQR LKERYYGHVD VLGYVGAYTF AQHLQQRLPR YEKMFRQAGH
310 320 330 340 350
ANQIDWRLLA AMGYQESLWQ PNATSKTGVR GLMMLTQRTA QSVGVSNRLD
360 370 380 390 400
PKQSIDGGAR YFVQIHQQLP ESIQEPDRTW FALAAYNVGG GHLEDARKLT
410 420 430 440 450
EAEGLDPNKW MDVQKILPRL AQKQWYSKTR YGYARGGEPV HFVRNVRRYY
460 470 480
DILTWVTQPQ LEGTQVAENG IHLPGIDKRT LDEQTPPL
Length:488
Mass (Da):54,830
Last modified:May 29, 2007 - v1
Checksum:iFC64949BEDB248EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000680 Genomic DNA. Translation: ABP86167.1.
RefSeqiWP_012019469.1. NC_009439.1.

Genome annotation databases

EnsemblBacteriaiABP86167; ABP86167; Pmen_3415.
GeneIDi5105887.
KEGGipmy:Pmen_3415.
PATRICi19913454. VBIPseMen131592_3465.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000680 Genomic DNA. Translation: ABP86167.1.
RefSeqiWP_012019469.1. NC_009439.1.

3D structure databases

ProteinModelPortaliA4XXV1.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP86167; ABP86167; Pmen_3415.
GeneIDi5105887.
KEGGipmy:Pmen_3415.
PATRICi19913454. VBIPseMen131592_3465.

Phylogenomic databases

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
KOiK18691.
OMAiKYGYARG.
OrthoDBiPOG091H03Q9.

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

Entry informationi

Entry nameiMLTF_PSEMY
AccessioniPrimary (citable) accession number: A4XXV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: May 29, 2007
Last modified: November 30, 2016
This is version 62 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.