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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
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 sitei312UniRule 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:APP7_1417
OrganismiActinobacillus pleuropneumoniae serotype 7 (strain AP76)
Taxonomic identifieri537457 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus
Proteomesi
  • UP000001226 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 – 18UniRule annotationAdd BLAST18
ChainiPRO_000035391419 – 483Membrane-bound lytic murein transglycosylase FAdd BLAST465

Structurei

3D structure databases

ProteinModelPortaliB3GYE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 267Non-LT domainUniRule annotationAdd BLAST249
Regioni269 – 483LT domainUniRule annotationAdd BLAST215

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

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. 1 hit.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

B3GYE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGLIARFIA GFALLLWAWD MVFPWQQLMQ AEENRYNQIQ QRKILRVGMV
60 70 80 90 100
NHPLSYFIGA EGTAGIEYEL AKSFANYLDV RLDIKTFDNS EQLFSALKDN
110 120 130 140 150
KVDIAAAGLL YQPELSKQFQ IGSAYYSASW QVVYKKGSNR PYKLSELEGD
160 170 180 190 200
LIIPAGSAVL PILQRLKEDN PKLSWQTTNQ FTQEELLLQV AEGKIPYTVG
210 220 230 240 250
ISVDISAAQH IRPNIAVGFD LTDEAPVLWY LPNSSYSELQ AAVLDFMNHA
260 270 280 290 300
NETGLISRIE EKYFNHLAHF DYVDIQSYLK AIKLVLPKYQ SLFEKYRGDL
310 320 330 340 350
EWQMLAAIAY QESHWDPNAT SPTGVRGMMM LTRDTAERMK ITDRTSAEQS
360 370 380 390 400
IRAGSEYLHM LMRQIPETVP KEDRIWYGLA AYNMGLGHLL DVRRLTRQLG
410 420 430 440 450
GNPDNWLDVK KNLPLLAEKR HYSGLKYGYA RGFEAFQYVE NIRRYYSSII
460 470 480
NHQRVEEQQI QNNEEQSSVP QEISKESDST LKE
Length:483
Mass (Da):55,510
Last modified:July 22, 2008 - v1
Checksum:i25F2C7B682A0D0C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001091 Genomic DNA. Translation: ACE62069.1.
RefSeqiWP_005608600.1. NC_010939.1.

Genome annotation databases

EnsemblBacteriaiACE62069; ACE62069; APP7_1417.
KEGGiapa:APP7_1417.
PATRICi20756529. VBIActPle116979_1450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001091 Genomic DNA. Translation: ACE62069.1.
RefSeqiWP_005608600.1. NC_010939.1.

3D structure databases

ProteinModelPortaliB3GYE5.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACE62069; ACE62069; APP7_1417.
KEGGiapa:APP7_1417.
PATRICi20756529. VBIActPle116979_1450.

Phylogenomic databases

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. 1 hit.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMLTF_ACTP7
AccessioniPrimary (citable) accession number: B3GYE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 22, 2008
Last modified: November 30, 2016
This is version 52 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

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.