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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
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 sitei330UniRule 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:VIBHAR_01149
OrganismiVibrio campbellii (strain ATCC BAA-1116 / BB120)
Taxonomic identifieri338187 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000008152 Componenti: Chromosome I

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 – 24UniRule annotationAdd BLAST24
ChainiPRO_000035399225 – 534Membrane-bound lytic murein transglycosylase FAdd BLAST510

Proteomic databases

PRIDEiA7MSG2

Interactioni

Protein-protein interaction databases

STRINGi338187.VIBHAR_01149

Structurei

3D structure databases

ProteinModelPortaliA7MSG2
SMRiA7MSG2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni25 – 285Non-LT domainUniRule annotationAdd BLAST261
Regioni287 – 534LT domainUniRule annotationAdd BLAST248

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.

A7MSG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQISQFNRLK RSALLFASVL LLSACQIESE PKSEFEQIQE RGVLRVGTLN
60 70 80 90 100
NQLSYYIGPD GPAGLDYELA RKFAEQLGVK LEIRPAFRQA ELFPALKKGD
110 120 130 140 150
IDIIATGLNQ TSQAVQRFRP GPAYYYVSQQ VVYKKGQLRP RDVDQLIKYQ
160 170 180 190 200
ESKDEKAGNE DSNAGAETLQ IVEQSQFVPT LTALQKEHPE LQFEIIGDAD
210 220 230 240 250
TRDLLKHVST GELRFTVTDS VELSLAQRLY PDLALAFELT EDQPVSWFTR
260 270 280 290 300
RSEDESLYAM LIEFFGNIKQ SGELATLEEK YIGHIEAFDY VDTRAFIRAL
310 320 330 340 350
DNTLPKWSPL FQKYSEEFDW RLIAALAYQE SHWKPKAKSP TGVRGMMMLT
360 370 380 390 400
LPTAKSVGVT DRLDPEQSVR GGVEYLRRIV ARVPDSINEH EKIWFALASY
410 420 430 440 450
NVGYGHMMDA RRLTKAQGGD PNAWADVKER LPLLRQKRYY SQTRYGYARG
460 470 480 490 500
DEARNYVENI RRYYQSIIGH VSQKPAIDED TEDLQVIPPL DPNLLVSGAV
510 520 530
ETLAEQVSGA VEVTPPPEEN APQEAEQTPV PKAE
Length:534
Mass (Da):60,517
Last modified:October 2, 2007 - v1
Checksum:i67B9B189524ABEA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000789 Genomic DNA Translation: ABU70139.1
RefSeqiWP_005533708.1, NC_022269.1

Genome annotation databases

EnsemblBacteriaiABU70139; ABU70139; VIBHAR_01149
GeneIDi5554041
KEGGivca:M892_07200
vha:VIBHAR_01149
PATRICifig|338187.25.peg.1479

Similar proteinsi

Entry informationi

Entry nameiMLTF_VIBCB
AccessioniPrimary (citable) accession number: A7MSG2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 2, 2007
Last modified: May 23, 2018
This is version 66 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

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