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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
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 sitei302UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processCell 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:Sputcn32_2643
OrganismiShewanella putrefaciens (strain CN-32 / ATCC BAA-453)
Taxonomic identifieri319224 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000006699 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 – 22UniRule annotationAdd BLAST22
ChainiPRO_500024165323 – 477Membrane-bound lytic murein transglycosylase FAdd BLAST455

Proteomic databases

PRIDEiA4Y8T1

Interactioni

Protein-protein interaction databases

STRINGi319224.Sputcn32_2643

Structurei

3D structure databases

ProteinModelPortaliA4Y8T1
SMRiA4Y8T1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 257Non-LT domainUniRule annotationAdd BLAST235
Regioni258 – 477LT domainUniRule annotationAdd BLAST220

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
OrthoDBiPOG091H03Q9

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
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
PS51257 PROKAR_LIPOPROTEIN, 1 hit

Sequencei

Sequence statusi: Complete.

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

A4Y8T1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRFLLIIIL GFLLTACQQV TVDEPEFVPH QLTELRVGTL YGPQIYMTSG
60 70 80 90 100
QGNSGFDYDM ALRFAEYLNV PLKMVPYTNR SELYDALKKN DIDIIAAGMT
110 120 130 140 150
ETPARREQFR LGPPLYRVNQ VLVYREGVAA PKDISKLKGR ITIIADSAFV
160 170 180 190 200
ETLTQLQKHH PSLVWDQVTD KDSEELLAMI ANKEIDYTIA DSSSVQINRR
210 220 230 240 250
YLPDLRSGPV LEEKLDVVWL LPPTHSDALM SQLLAFWHQE KLAGTLDHLN
260 270 280 290 300
EKYFGHVKRF DYIDTRAFLR AIETVLPRYR QLFETHAGDL DWRKLAATSY
310 320 330 340 350
QESHWNPHAR SPTGVRGMMM LTEPTAKEIG ITNRLDAEES IRGGAAYLRD
360 370 380 390 400
MINRLPESIP ESQRMWFALA SYNIGYAHVE DARKLAESME LNPNAWRDLK
410 420 430 440 450
KVLPLLQKRK YYQKTRYGYA RGSEAVHYVD SIRRYYDTLV WVDNQSKQPM
460 470
PEDEQNDLIA EELPSMPAGS LSPDQPK
Length:477
Mass (Da):54,788
Last modified:May 29, 2007 - v1
Checksum:iB7691EAABE33CAFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000681 Genomic DNA Translation: ABP76364.1
RefSeqiWP_011788713.1, NC_009438.1

Genome annotation databases

EnsemblBacteriaiABP76364; ABP76364; Sputcn32_2643
KEGGispc:Sputcn32_2643

Similar proteinsi

Entry informationi

Entry nameiMLTF_SHEPC
AccessioniPrimary (citable) accession number: A4Y8T1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: May 29, 2007
Last modified: May 23, 2018
This is version 68 of the entry and version 1 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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