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A7MGZ5 (MLTF_CROS8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Membrane-bound lytic murein transglycosylase F

EC=4.2.2.n1
Alternative name(s):
Murein lyase F
Gene names
Name:mltF
Ordered Locus Names:ESA_00703
OrganismCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_02016

Catalytic activity

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. HAMAP-Rule MF_02016

Subcellular location

Cell outer membrane; Peripheral membrane protein. Note: Attached to the inner leaflet of the outer membrane By similarity. HAMAP-Rule MF_02016

Domain

The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain By similarity. HAMAP-Rule MF_02016

Sequence similarities

In the N-terminal section; belongs to the bacterial solute-binding protein 3 family.

In the C-terminal section; belongs to the transglycosylase Slt family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell outer membrane
Membrane
   DomainSignal
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcell wall macromolecule catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbon-oxygen lyase activity, acting on polysaccharides

Inferred from electronic annotation. Source: UniProtKB-EC

lytic transglycosylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 519487Membrane-bound lytic murein transglycosylase F HAMAP-Rule MF_02016
PRO_0000353936

Regions

Region33 – 269237Non-LT domain By similarity
Region270 – 519250LT domain By similarity

Sites

Active site3141 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7MGZ5 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 818FB065D8B03B13

FASTA51957,617
        10         20         30         40         50         60 
MKKLKLNYLL IGVVTLLLAV ALWPAIPWSG KADNRIAAIQ ARGVLRVSTI ATPLTMYRAG 

        70         80         90        100        110        120 
DTMSGLDYEL SQAFADYLGV KLKITVRQNI SQLFDDLDNN DADLLAAGLV YNEARSQHYQ 

       130        140        150        160        170        180 
AGPIYYSVSQ QMVYRVGSLR PRSLASIKEG QLTIAPGHVA QSELEQLKAS KYPDLTWRVD 

       190        200        210        220        230        240 
PKLSSNELML QVAQGTLDYT IADSVAISLF QRVHPQLAVA LDLSDEQPVT WFSRRSSDNS 

       250        260        270        280        290        300 
LSAALLDFFN QINEDGTLAR LEEKYLGHGN DFDYVDTRSF LRAVDSVLPE LQPLFEKYAT 

       310        320        330        340        350        360 
DIDWRLLAAI SYQESHWDSQ ATSPTGVRGL MMLTRNTAQS LGLTDRLDAE QSISGGARYL 

       370        380        390        400        410        420 
KDMMSKVPES VPEEERIWFA LAAYNMGYAH MLDARALTAK QKGNPDSWSD VKQRLPLLSQ 

       430        440        450        460        470        480 
RPYYSKLTYG YARGHEAYAY VENIRKYQIS LVGYLLEKEK QAAAAAQPKL VQSYPTNITP 

       490        500        510 
QGLFPSPFSS LPLGPFSQAG AGGKTHSALP NTLSPVSPR 

« Hide

References

[1]"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-894.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU75981.1.
RefSeqYP_001436817.1. NC_009778.1.

3D structure databases

ProteinModelPortalA7MGZ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290339.ESA_00703.

Protein family/group databases

CAZyGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU75981; ABU75981; ESA_00703.
GeneID5548883.
KEGGesa:ESA_00703.
PATRIC20393627. VBICroSak107175_0621.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4623.
HOGENOMHOG000218316.
OMANIRRYYD.
OrthoDBEOG62C9FB.

Enzyme and pathway databases

BioCycCSAK290339:GJ80-697-MONOMER.

Family and domain databases

HAMAPMF_02016. MltF.
InterProIPR023346. Lysozyme-like_dom.
IPR023703. MltF.
IPR001638. SBP_bac_3.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamPF00497. SBP_bac_3. 1 hit.
PF01464. SLT. 1 hit.
[Graphical view]
SMARTSM00062. PBPb. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMLTF_CROS8
AccessionPrimary (citable) accession number: A7MGZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 2, 2007
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families