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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Shewanella baltica (strain OS195)
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 sitei302 – 3021UniRule 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

BioCyciSBAL399599:GH6B-3240-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:Sbal195_3139
OrganismiShewanella baltica (strain OS195)
Taxonomic identifieri399599 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000000770 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 – 2222UniRule annotationAdd
BLAST
Chaini23 – 476454Membrane-bound lytic murein transglycosylase FPRO_5000296743Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA9KWW4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 257235Non-LT domainUniRule annotationAdd
BLAST
Regioni258 – 476219LT 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

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. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A9KWW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRFLFALIL GFLLTACQQV TVDETEFVPK KLTELRVGTL YGPQIYMTSG
60 70 80 90 100
QGDSGFDYDM AVLFAEYLDV PLKMVPYTNR TELYEALKKN EIDLIAAGMT
110 120 130 140 150
ETPARREQFR LGPPLYRVNQ VLVYREGMPA PKDISDLKGK ITVIADSSFV
160 170 180 190 200
ETLTQLQKHY PTLVWDQITD KDSEELLAMI ANKEIDYTIA DSSSVQINRR
210 220 230 240 250
YLPDLRSGPV LEEKLDVVWL LPPTRSDELM SQLLAFWHQE KLAGTLDHLN
260 270 280 290 300
EKYFGHVKRF DYVDTRAFIR AIETVLPRYR QLFETHAGNL DWRKLAATSY
310 320 330 340 350
QESHWNPHAR SATGVRGMMM LTQPTAKEIG ITNRLDAEES IRGGAAYLND
360 370 380 390 400
MINRLPESIP ESQRMWFALA SYNIGYAHVE DARKLAESME LNPNAWRDLK
410 420 430 440 450
KVLPLLQKRK YYQKTRYGYA RGSEAVHYVD SIRRYYDTLV WVDNQSKQQN
460 470
PEEEPSDLAS EEPAIPAGTL SPEQPK
Length:476
Mass (Da):54,652
Last modified:February 5, 2008 - v1
Checksum:i5CBC292735E3798C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000891 Genomic DNA. Translation: ABX50301.1.
RefSeqiWP_006082473.1. NC_009997.1.

Genome annotation databases

EnsemblBacteriaiABX50301; ABX50301; Sbal195_3139.
GeneIDi11773196.
KEGGisbn:Sbal195_3139.
sbt:Sbal678_3145.
PATRICi23472577. VBISheBal33754_3245.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000891 Genomic DNA. Translation: ABX50301.1.
RefSeqiWP_006082473.1. NC_009997.1.

3D structure databases

ProteinModelPortaliA9KWW4.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX50301; ABX50301; Sbal195_3139.
GeneIDi11773196.
KEGGisbn:Sbal195_3139.
sbt:Sbal678_3145.
PATRICi23472577. VBISheBal33754_3245.

Phylogenomic databases

HOGENOMiHOG000218316.
KOiK18691.
OMAiYYDILTW.
OrthoDBiEOG62C9FB.

Enzyme and pathway databases

BioCyciSBAL399599:GH6B-3240-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. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: OS195.

Entry informationi

Entry nameiMLTF_SHEB9
AccessioniPrimary (citable) accession number: A9KWW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: February 5, 2008
Last modified: March 16, 2016
This is version 57 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.