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Protein

Membrane-bound lytic murein transglycosylase F

Gene

mltF

Organism
Haemophilus somnus (strain 129Pt) (Histophilus somni)
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)DescriptionActionsGraphical viewLength
Active sitei311UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cell 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:HS_1004
OrganismiHaemophilus somnus (strain 129Pt) (Histophilus somni)
Taxonomic identifieri205914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
Proteomesi
  • UP000001970 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18UniRule annotationAdd BLAST18
ChainiPRO_000035394319 – 482Membrane-bound lytic murein transglycosylase FAdd BLAST464

Interactioni

Protein-protein interaction databases

STRINGi205914.HS_1004.

Structurei

3D structure databases

ProteinModelPortaliQ0I361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 266Non-LT domainUniRule annotationAdd BLAST248
Regioni267 – 482LT domainUniRule annotationAdd BLAST216

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.
OrthoDBiPOG091H03Q9.

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

Sequencei

Sequence statusi: Complete.

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

Q0I361-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGLFIRIVL AICLSLWAID MVFPWQQIVR SKQNYHTTIQ ERQKLIVGTI
60 70 80 90 100
NNPVSYFIGT NGETGLEYEL SKAFANYLNV DLEMFPLNSA DALFQALAQG
110 120 130 140 150
KIDIAAASLF YQQDRSEKFK LGPAYHAASW QLTYRKGERR PITLENLSGK
160 170 180 190 200
LVIPANSALN NILLAKKEKY PSLTWETSEL SQEELLFQVA EGKIDYTIAT
210 220 230 240 250
STEVSVNQQI KPQIAIAFNV TDEFTVHWYL SDKGSSELQA ALLDFMNSAI
260 270 280 290 300
ENGLIARIEE KYFNHLNQFD YVDTRSYLNA IETVLPKYAP LFEKYKGDLD
310 320 330 340 350
WRLLAAISYQ ESHWNPEATS PTGVRGMMML TKATADRMNI TNRLDPEQSI
360 370 380 390 400
KAGSEYLHLL LKQMPDTILK EDRIWFALAA YNMGLGHLLD VRRLTKQLGG
410 420 430 440 450
NPDNWLEVKK NLPLLAQKRY FTHLKYGYAR GYEAFQYVEN IRRYMNSIMN
460 470 480
YYRLQQNQQD RQDRYENENN DVISTQTQQE QR
Length:482
Mass (Da):55,694
Last modified:November 25, 2008 - v2
Checksum:i801A1B075FC60B0E
GO

Sequence cautioni

The sequence ABI25279 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI25279.1. Different initiation.
RefSeqiWP_041604224.1. NC_008309.1.

Genome annotation databases

EnsemblBacteriaiABI25279; ABI25279; HS_1004.
KEGGihso:HS_1004.
PATRICi20282031. VBIHaeSom53361_1052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI25279.1. Different initiation.
RefSeqiWP_041604224.1. NC_008309.1.

3D structure databases

ProteinModelPortaliQ0I361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi205914.HS_1004.

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI25279; ABI25279; HS_1004.
KEGGihso:HS_1004.
PATRICi20282031. VBIHaeSom53361_1052.

Phylogenomic databases

eggNOGiENOG4105CHQ. Bacteria.
COG4623. LUCA.
HOGENOMiHOG000218316.
KOiK18691.
OrthoDBiPOG091H03Q9.

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

Entry informationi

Entry nameiMLTF_HAES1
AccessioniPrimary (citable) accession number: Q0I361
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 69 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

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.