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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionLyase
Biological processCell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciAPLE416269:G1G87-1442-MONOMER

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:APL_1366
OrganismiActinobacillus pleuropneumoniae serotype 5b (strain L20)
Taxonomic identifieri416269 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus
Proteomesi
  • UP000001432 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

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18UniRule annotationAdd BLAST18
ChainiPRO_000035391319 – 483Membrane-bound lytic murein transglycosylase FAdd BLAST465

Proteomic databases

PRIDEiA3N214

Interactioni

Protein-protein interaction databases

STRINGi416269.APL_1366

Structurei

3D structure databases

ProteinModelPortaliA3N214
SMRiA3N214
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

eggNOGiENOG4105CHQ Bacteria
COG4623 LUCA
HOGENOMiHOG000218316
KOiK18691

Family and domain databases

HAMAPiMF_02016 MltF, 1 hit
InterProiView protein in InterPro
IPR023346 Lysozyme-like_dom_sf
IPR023703 MltF
IPR001638 Solute-binding_3/MltF_N
IPR000189 Transglyc_AS
IPR008258 Transglycosylase_SLT_dom_1
PfamiView protein in Pfam
PF00497 SBP_bac_3, 1 hit
PF01464 SLT, 1 hit
SMARTiView protein in SMART
SM00062 PBPb, 1 hit
SUPFAMiSSF53955 SSF53955, 1 hit
PROSITEiView protein in PROSITE
PS00922 TRANSGLYCOSYLASE, 1 hit

Sequencei

Sequence statusi: Complete.

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

A3N214-1 [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
VSVDISAAQH IRPNIAVGFD LTDEAPVLWY LPNSSYSELQ AAVLDFMNHA
260 270 280 290 300
NETGLISRIE EKYFNHLAHF DYVDIQSYLK AIKLVLPKYQ SLFEKYCGDL
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 QNNEEQPSVP QEISKESDST LKE
Length:483
Mass (Da):55,453
Last modified:November 25, 2008 - v2
Checksum:i8E86EBCEC499662F
GO

Sequence cautioni

The sequence ABN74450 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000569 Genomic DNA Translation: ABN74450.1 Different initiation.
RefSeqiWP_009874919.1, NC_009053.1

Genome annotation databases

EnsemblBacteriaiABN74450; ABN74450; APL_1366
GeneIDi4849619
KEGGiapl:APL_1366
PATRICifig|416269.6.peg.1424

Similar proteinsi

Entry informationi

Entry nameiMLTF_ACTP2
AccessioniPrimary (citable) accession number: A3N214
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: May 23, 2018
This is version 68 of the entry and version 2 of the sequence. See 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

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