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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Escherichia coli O157:H7
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 sitei314UniRule 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:Z3838, ECs3424
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 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 – 21UniRule annotationAdd BLAST21
ChainiPRO_000035392822 – 518Membrane-bound lytic murein transglycosylase FAdd BLAST497

Interactioni

Protein-protein interaction databases

STRINGi155864.Z3838

Structurei

3D structure databases

ProteinModelPortaliQ8XA45
SMRiQ8XA45
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 269Non-LT domainUniRule annotationAdd BLAST248
Regioni270 – 518LT domainUniRule annotationAdd BLAST249

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

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, 2 hits
PROSITEiView protein in PROSITE
PS00922 TRANSGLYCOSYLASE, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q8XA45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLKINYLF IGILALLLAV ALWPSIPWFG KADNRIAAIQ ARGELRVSTI
60 70 80 90 100
HTPLTYNEIN GKPFGLDYEL AKQFADYLGV KLKVTVRQNI SQLFDDLDNG
110 120 130 140 150
NADLLAAGLV YNSERVKNYQ PGPTYYSVSQ QLVYKVGQYR PRTLGNLTAE
160 170 180 190 200
QLTVAPGHVV VNDLQTLKET KFPELSWKVD DKKGSAELME DVIEGKLDYT
210 220 230 240 250
IADSVAISLF QRVHPELAVA LDITDEQPVT WFSPLDGDNT LSAALLDFFN
260 270 280 290 300
EMNEDGTLAR IEEKYLGHGD DFDYVDTRTF LRAVDAVLPQ LKPLFEKYAE
310 320 330 340 350
EIDWRLLAAI AYQESHWDAQ ATSPTGVRGM MMLTKNTAQS LGITDRTDAE
360 370 380 390 400
QSISGGVRYL QDMMSKVPES VPENERIWFA LAAYNMGYAH MQDARALTAK
410 420 430 440 450
TKGNPDSWAD VKQRLPLLSQ KPYYSKLTYG YARGHEAYAY VENIRKYQIS
460 470 480 490 500
LVGYLQEKEK QATEAAMQLA QDYPAVSPTE LGKEKFPFLS FLSQSSSNYL
510
THSPSLLFSR KGSEEKQN
Length:518
Mass (Da):58,317
Last modified:November 25, 2008 - v2
Checksum:i6155ABE8531471BA
GO

Sequence cautioni

The sequence AAG57672 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB36847 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA Translation: AAG57672.1 Different initiation.
BA000007 Genomic DNA Translation: BAB36847.1 Different initiation.
PIRiD85901
H91056
RefSeqiNP_311451.2, NC_002695.1
WP_000734215.1, NZ_NOKN01000002.1

Genome annotation databases

EnsemblBacteriaiAAG57672; AAG57672; Z3838
BAB36847; BAB36847; BAB36847
GeneIDi914913
KEGGiece:Z3838
ecs:ECs3424
PATRICifig|386585.9.peg.3578

Similar proteinsi

Entry informationi

Entry nameiMLTF_ECO57
AccessioniPrimary (citable) accession number: Q8XA45
Secondary accession number(s): Q7ABK4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: April 25, 2018
This is version 105 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
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Main funding by: National Institutes of Health