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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Pseudomonas putida (strain KT2440)
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 sitei314 – 3141UniRule 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

BioCyciPPUT160488:GIXO-1068-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:PP_1036
OrganismiPseudomonas putida (strain KT2440)
Taxonomic identifieri160488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000000556 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

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929UniRule annotationAdd
BLAST
Chaini30 – 485456Membrane-bound lytic murein transglycosylase FPRO_0000353964Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ88P17.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 267238Non-LT domainUniRule annotationAdd
BLAST
Regioni268 – 485218LT 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.
OMAiKYGYARG.

Family and domain databases

HAMAPiMF_02016. MltF. 1 hit.
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.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q88P17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFAHTALRQR CAKWLLATGL FLLLGACVEK PSTLERVKED GVLRVITRNS
60 70 80 90 100
PATYFQDRNG ETGFEYELVQ HFADDLGVKL QIETADNLDE LYDALGKPSG
110 120 130 140 150
PVLAAAGLVS SERRKTQVRY SHPYLEVTPQ VIYRNGRPRP TGAKGLVGKK
160 170 180 190 200
IMVLKGSSHA DQLAELKKQY PALQYEESDA VEVVDLLRMV DEGQIDLTLV
210 220 230 240 250
DSNELAMNQV YFPNVRVAFD LGETRDQRWA VAAGEDNSLL NEINEYLDKA
260 270 280 290 300
QKNGTLQRLK DRYYGHVDVL GYVGAYTFAQ HLQQRLPKYE KHFKSYAKVE
310 320 330 340 350
QVDWRLLAAI GYQESMWQPE VTSKTGVRGL MMLTQRTAQA MGVSNRLDPR
360 370 380 390 400
QSIQGGAKYF MKIKEELDDS IKEPDRTWFA LAAYNVGGGH LEDARTLAKR
410 420 430 440 450
EKLNPNKWLD VKKMLPRLAQ KQWYRQTKYG YARGGEPVHF VANIRRYYDI
460 470 480
LTWVTQPQLE GQVAEGNLHV PGVNKDKPAD KSSPM
Length:485
Mass (Da):55,044
Last modified:November 25, 2008 - v2
Checksum:i674FB02FB5DEDF3E
GO

Sequence cautioni

The sequence AAN66661 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015451 Genomic DNA. Translation: AAN66661.1. Different initiation.
RefSeqiNP_743197.2. NC_002947.4.
WP_020193355.1. NC_002947.4.

Genome annotation databases

EnsemblBacteriaiAAN66661; AAN66661; PP_1036.
GeneIDi1044173.
KEGGippu:PP_1036.
PATRICi19940226. VBIPsePut30601_1099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015451 Genomic DNA. Translation: AAN66661.1. Different initiation.
RefSeqiNP_743197.2. NC_002947.4.
WP_020193355.1. NC_002947.4.

3D structure databases

ProteinModelPortaliQ88P17.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN66661; AAN66661; PP_1036.
GeneIDi1044173.
KEGGippu:PP_1036.
PATRICi19940226. VBIPsePut30601_1099.

Phylogenomic databases

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
KOiK18691.
OMAiKYGYARG.

Enzyme and pathway databases

BioCyciPPUT160488:GIXO-1068-MONOMER.

Family and domain databases

HAMAPiMF_02016. MltF. 1 hit.
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.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMLTF_PSEPK
AccessioniPrimary (citable) accession number: Q88P17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: September 7, 2016
This is version 83 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.