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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: 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 sitei329 – 3291UniRule 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

BioCyciVPAR223926:GHK4-684-MONOMER.

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

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424UniRule annotationAdd
BLAST
Chaini25 – 525501Membrane-bound lytic murein transglycosylase FPRO_0000353993Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi223926.VP0665.

Structurei

3D structure databases

ProteinModelPortaliQ87RW1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 284260Non-LT domainUniRule annotationAdd
BLAST
Regioni286 – 525240LT 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

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
KOiK18691.
OMAiYYDILTW.
OrthoDBiEOG62C9FB.

Family and domain databases

HAMAPiMF_02016. MltF.
InterProiIPR023346. Lysozyme-like_dom.
IPR023703. MltF.
IPR001638. Solute-binding_3/MltF_N.
IPR000189. Transglyc_AS.
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. 2 hits.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

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 BAC58928.1 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.
PATRICi20139532. VBIVibPar50997_0633.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ87RW1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi223926.VP0665.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC58928; BAC58928; BAC58928.
GeneIDi1188140.
KEGGivpa:VP0665.
PATRICi20139532. VBIVibPar50997_0633.

Phylogenomic databases

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
KOiK18691.
OMAiYYDILTW.
OrthoDBiEOG62C9FB.

Enzyme and pathway databases

BioCyciVPAR223926:GHK4-684-MONOMER.

Family and domain databases

HAMAPiMF_02016. MltF.
InterProiIPR023346. Lysozyme-like_dom.
IPR023703. MltF.
IPR001638. Solute-binding_3/MltF_N.
IPR000189. Transglyc_AS.
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. 2 hits.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
    Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
    Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RIMD 2210633.

Entry informationi

Entry nameiMLTF_VIBPA
AccessioniPrimary (citable) accession number: Q87RW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: May 11, 2016
This is version 78 of the entry and version 2 of the sequence. [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

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.