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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 3 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.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:PA3764
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3764.

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 – 32UniRule annotationAdd BLAST32
ChainiPRO_000035395733 – 490Membrane-bound lytic murein transglycosylase FAdd BLAST458

Proteomic databases

PaxDbiQ9HXN1.

Structurei

Secondary structure

1490
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 42Combined sources8
Beta strandi44 – 52Combined sources9
Turni53 – 55Combined sources3
Beta strandi56 – 59Combined sources4
Beta strandi62 – 64Combined sources3
Helixi66 – 78Combined sources13
Beta strandi81 – 89Combined sources9
Helixi90 – 97Combined sources8
Beta strandi104 – 106Combined sources3
Beta strandi120 – 122Combined sources3
Beta strandi127 – 129Combined sources3
Beta strandi131 – 136Combined sources6
Helixi145 – 148Combined sources4
Beta strandi153 – 156Combined sources4
Helixi160 – 171Combined sources12
Beta strandi178 – 182Combined sources5
Helixi185 – 193Combined sources9
Beta strandi196 – 203Combined sources8
Helixi204 – 210Combined sources7
Turni211 – 213Combined sources3
Beta strandi217 – 222Combined sources6
Beta strandi227 – 229Combined sources3
Beta strandi232 – 237Combined sources6
Helixi240 – 254Combined sources15
Helixi257 – 266Combined sources10
Helixi268 – 272Combined sources5
Helixi274 – 286Combined sources13
Helixi288 – 302Combined sources15
Helixi306 – 317Combined sources12
Beta strandi326 – 328Combined sources3
Turni331 – 334Combined sources4
Helixi337 – 343Combined sources7
Helixi351 – 368Combined sources18
Helixi377 – 388Combined sources12
Helixi390 – 402Combined sources13
Helixi410 – 416Combined sources7
Helixi417 – 421Combined sources5
Helixi423 – 426Combined sources4
Beta strandi429 – 431Combined sources3
Helixi436 – 454Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OWDX-ray2.21A33-459[»]
4OYVX-ray2.31A28-460[»]
4OZ9X-ray2.24A33-460[»]
4P0GX-ray1.65A28-460[»]
4P11X-ray1.89A28-460[»]
5A5XX-ray1.80A38-490[»]
B40-490[»]
5AA1X-ray2.89A/B/C/D8-490[»]
5AA2X-ray2.80A/B/C/D8-490[»]
5AA3X-ray3.20A/B/C/D/E/F/G/H/I/J/K/L8-490[»]
ProteinModelPortaliQ9HXN1.
SMRiQ9HXN1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 269Non-LT domainUniRule annotationAdd BLAST237
Regioni270 – 490LT domainUniRule annotationAdd BLAST221

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.
InParanoidiQ9HXN1.
KOiK18691.
OMAiKYGYARG.

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.

Q9HXN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFALTAYRLR CAAWLLATGI FLLLAGCSEA KAPTALERVQ KEGVLRVITR
60 70 80 90 100
NSPATYFQDR NGETGFEYEL AKRFAERLGV ELKIETADNL DDLYAQLSRE
110 120 130 140 150
GGPALAAAGL TPGREDDASV RYSHTYLDVT PQIIYRNGQQ RPTRPEDLVG
160 170 180 190 200
KRIMVLKGSS HAEQLAELKK QYPELKYEES DAVEVVDLLR MVDVGDIDLT
210 220 230 240 250
LVDSNELAMN QVYFPNVRVA FDFGEARGLA WALPGGDDDS LMNEVNAFLD
260 270 280 290 300
QAKKEGLLQR LKDRYYGHVD VLGYVGAYTF AQHLQQRLPR YESHFKQSGK
310 320 330 340 350
QLDTDWRLLA AIGYQESLWQ PGATSKTGVR GLMMLTNRTA QAMGVSNRLD
360 370 380 390 400
PKQSIQGGSK YFVQIRSELP ESIKEPDRSW FALAAYNIGG AHLEDARKMA
410 420 430 440 450
EKEGLNPNKW LDVKKMLPRL AQKQWYAKTR YGYARGGETV HFVQNVRRYY
460 470 480 490
DILTWVTQPQ MEGSQIAESG LHLPGVNKTR PEEDSGDEKL
Length:490
Mass (Da):55,227
Last modified:November 25, 2008 - v2
Checksum:i191CB459DBB67121
GO

Sequence cautioni

The sequence AAG07151 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG07151.1. Different initiation.
PIRiC83175.
RefSeqiNP_252453.1. NC_002516.2.
WP_003104806.1. NZ_ASJY01000606.1.

Genome annotation databases

EnsemblBacteriaiAAG07151; AAG07151; PA3764.
GeneIDi880530.
KEGGipae:PA3764.
PATRICi19842163. VBIPseAer58763_3939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG07151.1. Different initiation.
PIRiC83175.
RefSeqiNP_252453.1. NC_002516.2.
WP_003104806.1. NZ_ASJY01000606.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OWDX-ray2.21A33-459[»]
4OYVX-ray2.31A28-460[»]
4OZ9X-ray2.24A33-460[»]
4P0GX-ray1.65A28-460[»]
4P11X-ray1.89A28-460[»]
5A5XX-ray1.80A38-490[»]
B40-490[»]
5AA1X-ray2.89A/B/C/D8-490[»]
5AA2X-ray2.80A/B/C/D8-490[»]
5AA3X-ray3.20A/B/C/D/E/F/G/H/I/J/K/L8-490[»]
ProteinModelPortaliQ9HXN1.
SMRiQ9HXN1.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Proteomic databases

PaxDbiQ9HXN1.

Protocols and materials databases

DNASUi880530.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07151; AAG07151; PA3764.
GeneIDi880530.
KEGGipae:PA3764.
PATRICi19842163. VBIPseAer58763_3939.

Organism-specific databases

PseudoCAPiPA3764.

Phylogenomic databases

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
InParanoidiQ9HXN1.
KOiK18691.
OMAiKYGYARG.

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_PSEAE
AccessioniPrimary (citable) accession number: Q9HXN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 96 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.