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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Shewanella sediminis (strain HAW-EB3)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei304 – 3041UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciSSED425104:GH7Q-3238-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:Ssed_3120
OrganismiShewanella sediminis (strain HAW-EB3)
Taxonomic identifieri425104 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000002015 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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515UniRule annotationAdd
BLAST
Chaini16 – 480465Membrane-bound lytic murein transglycosylase FPRO_5000278524Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi425104.Ssed_3120.

Structurei

3D structure databases

ProteinModelPortaliA8FY01.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 259244Non-LT domainUniRule annotationAdd
BLAST
Regioni260 – 480221LT domainUniRule annotationAdd
BLAST

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.
OMAiYYDILTW.
OrthoDBiEOG62C9FB.

Family and domain databases

HAMAPiMF_02016. MltF.
InterProiIPR023346. Lysozyme-like_dom.
IPR023703. MltF.
IPR001638. Solute-binding_3/MltF_N.
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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A8FY01-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLLFVLLT ITLLASCQKV SVEQTKVIPE PIKKTTLNVG TLYGAQIFVT
60 70 80 90 100
TGQGEAGFDF EMASRFAEYL KLELKMKPYS NISELYQALE SGEVDLLAAG
110 120 130 140 150
LADTPTRREK FRLGPPLYRV NQVLVYKQGT PIPKDVSTLE DNITVITDSS
160 170 180 190 200
FVETLSQLQK LYPELVWEQE KEKDSEELMA MIARGEITYT IADSSTFEIN
210 220 230 240 250
RRYLPELRAG PILKEKQAIV WLLPPKNSDQ LMSDLLTFWH YEKRSGTLAH
260 270 280 290 300
LNEKYFAHVK RFDYVDTRAF LRAIDNKLPK YKESFQHYAN GIDWRKLAAT
310 320 330 340 350
AYQESHWNPN ARSPTGVRGL MMLTLPTAKQ VGIKNRLDPI QSIKGGAKYL
360 370 380 390 400
NDILNRLPDS IPENQRMWFA LASYNIGYGH VEDARKLAQS MGLNPSAWRD
410 420 430 440 450
LKEVLPLLHK RKYYQRTRYG YARGNEAVHY VDSIRRYYDT LVWVDNQNQL
460 470 480
LIDEKASAEE SQLAEKIGGK QENLSGAQPQ
Length:480
Mass (Da):54,958
Last modified:November 13, 2007 - v1
Checksum:i3FAD170477F522D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA. Translation: ABV37724.1.
RefSeqiWP_012143454.1. NC_009831.1.

Genome annotation databases

EnsemblBacteriaiABV37724; ABV37724; Ssed_3120.
KEGGisse:Ssed_3120.
PATRICi23563995. VBISheSed62411_3314.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA. Translation: ABV37724.1.
RefSeqiWP_012143454.1. NC_009831.1.

3D structure databases

ProteinModelPortaliA8FY01.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi425104.Ssed_3120.

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV37724; ABV37724; Ssed_3120.
KEGGisse:Ssed_3120.
PATRICi23563995. VBISheSed62411_3314.

Phylogenomic databases

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
KOiK18691.
OMAiYYDILTW.
OrthoDBiEOG62C9FB.

Enzyme and pathway databases

BioCyciSSED425104:GH7Q-3238-MONOMER.

Family and domain databases

HAMAPiMF_02016. MltF.
InterProiIPR023346. Lysozyme-like_dom.
IPR023703. MltF.
IPR001638. Solute-binding_3/MltF_N.
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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HAW-EB3.

Entry informationi

Entry nameiMLTF_SHESH
AccessioniPrimary (citable) accession number: A8FY01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 13, 2007
Last modified: December 9, 2015
This is version 56 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.