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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
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 sitei329UniRule 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:VP0665
OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Taxonomic identifieri223926 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000002493 Componenti: Chromosome 1

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_000035399325 – 525Membrane-bound lytic murein transglycosylase FAdd BLAST501

Proteomic databases

PRIDEiQ87RW1

Interactioni

Protein-protein interaction databases

STRINGi223926.VP0665

Structurei

3D structure databases

ProteinModelPortaliQ87RW1
SMRiQ87RW1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni25 – 284Non-LT domainUniRule annotationAdd BLAST260
Regioni286 – 525LT domainUniRule annotationAdd BLAST240

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
PS51257 PROKAR_LIPOPROTEIN, 1 hit
PS00922 TRANSGLYCOSYLASE, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q87RW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIRHFNRLK RSVLLFASVL LLSACQIESQ PKSEFEKIQE RGVLRVGTLN
60 70 80 90 100
NQLSYYIGPD GPAGLDYELA RKFAEELGVK LEIKPAFRQA DLFPALKKGD
110 120 130 140 150
IDIIATGLNQ TSQAVKRFRP GPAYYYVSQQ VVYKKGQLRP RDIEQLIEYQ
160 170 180 190 200
ASKDSQSEED VNAGAQTLKI VEQSQYVPTL TALKKQYPEL QFEIVGDADT
210 220 230 240 250
RDLLKHVSTG ELRFTVTDSV ELSLAQRLYP DLALAFELTE DQPVSWFTRR
260 270 280 290 300
SEDESLYAML IEFFGNIKQS GELASLEEKY IGHIEAFDYV DTRAFIRALD
310 320 330 340 350
DKLPRWAPLF QKYSEEFDWR LIAALAYQES HWKPKAKSPT GVRGMMMLTL
360 370 380 390 400
PTAKSVGVTD RLNPEQSVRG GVEYLRRIVA RVPDTINEHE KIWFALASYN
410 420 430 440 450
IGYGHMMDAR RLTKAQGGDP NAWADVKDRL PLLRQKRYYS QTRYGYARGD
460 470 480 490 500
EARNYVENIR RYYQSIIGHV SQKPSIDEDT DDLQVIPPLN PELLISGAVE
510 520
TIAEEVSGAS DITNEVDEDL DQEEE
Length:525
Mass (Da):59,886
Last modified:November 25, 2008 - v2
Checksum:iB591DBC5D5574E35
GO

Sequence cautioni

The sequence BAC58928 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000031 Genomic DNA Translation: BAC58928.1 Different initiation.
RefSeqiNP_797044.1, NC_004603.1

Genome annotation databases

EnsemblBacteriaiBAC58928; BAC58928; BAC58928
GeneIDi1188140
KEGGivpa:VP0665
PATRICifig|223926.6.peg.633

Similar proteinsi

Entry informationi

Entry nameiMLTF_VIBPA
AccessioniPrimary (citable) accession number: Q87RW1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: May 23, 2018
This is version 89 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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