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Protein

Membrane-bound lytic murein transglycosylase C

Gene

mltC

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. May play a role in recycling of muropeptides during cell elongation and/or cell division.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

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 CUniRule annotation (EC:4.2.2.n1UniRule annotation)
Alternative name(s):
Murein lyase CUniRule annotation
Gene namesi
Name:mltCUniRule annotation
Ordered Locus Names:HS_1669
OrganismiHaemophilus somnus (strain 129Pt) (Histophilus somni)
Taxonomic identifieri205914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
Proteomesi
  • UP000001970 Componenti: Chromosome

Subcellular locationi

  • Cell outer membrane UniRule annotation; Lipid-anchor 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 – 15UniRule annotationAdd BLAST15
ChainiPRO_100006947816 – 363Membrane-bound lytic murein transglycosylase CAdd BLAST348

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi16N-palmitoyl cysteineUniRule annotation1
Lipidationi16S-diacylglycerol cysteineUniRule annotation1

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Protein-protein interaction databases

STRINGi205914.HS_1669.

Structurei

3D structure databases

ProteinModelPortaliQ0I513.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transglycosylase Slt family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106S48. Bacteria.
COG0741. LUCA.
HOGENOMiHOG000283572.
KOiK08306.
OMAiAIMQIES.
OrthoDBiPOG091H06EG.

Family and domain databases

HAMAPiMF_01616. MltC. 1 hit.
InterProiIPR023346. Lysozyme-like_dom.
IPR023664. Murein_transglycosylaseC.
IPR024570. Murein_transglycosylaseC_N.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[Graphical view]
PfamiPF11873. DUF3393. 1 hit.
PF01464. SLT. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
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.

Q0I513-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKYIVFAII PFLFACSSST LNDDYDEAFA KDTQGLDILT GQFSHNIDQI
60 70 80 90 100
WGVNELLVAS RKDYVKYTDN FYTRSHISFD EGSIMIETLG DKSRLYHSII
110 120 130 140 150
HTLLMGADAK GIDLFTSGDV PISSRPFLVG LVVDHKGKQV KNIATASNFA
160 170 180 190 200
NYLLQNKLQT RYLTNGNPVQ YVIIPMVANH VAVRAQRYLP LIRKAAGRYG
210 220 230 240 250
IDESLILGIM QTESSFNPYA ISYANAIGLM QVVPHTAGRD VFRLKGLNGQ
260 270 280 290 300
PSKKYLFNPA KNIDTGVAYL TLLRDKYLDG ITNPTSKRFA MISAYNSGAG
310 320 330 340 350
AVLRVFHNDR DIAINKINRL YPEQVYRILT TMHPSEQARN YLLKVDKAQK
360
SYRVIKNSES DLP
Length:363
Mass (Da):40,794
Last modified:October 3, 2006 - v1
Checksum:i7604D9FAAA8DB197
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI25937.1.
RefSeqiWP_011609814.1. NC_008309.1.

Genome annotation databases

EnsemblBacteriaiABI25937; ABI25937; HS_1669.
KEGGihso:HS_1669.
PATRICi20283495. VBIHaeSom53361_1747.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI25937.1.
RefSeqiWP_011609814.1. NC_008309.1.

3D structure databases

ProteinModelPortaliQ0I513.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi205914.HS_1669.

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI25937; ABI25937; HS_1669.
KEGGihso:HS_1669.
PATRICi20283495. VBIHaeSom53361_1747.

Phylogenomic databases

eggNOGiENOG4106S48. Bacteria.
COG0741. LUCA.
HOGENOMiHOG000283572.
KOiK08306.
OMAiAIMQIES.
OrthoDBiPOG091H06EG.

Family and domain databases

HAMAPiMF_01616. MltC. 1 hit.
InterProiIPR023346. Lysozyme-like_dom.
IPR023664. Murein_transglycosylaseC.
IPR024570. Murein_transglycosylaseC_N.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[Graphical view]
PfamiPF11873. DUF3393. 1 hit.
PF01464. SLT. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMLTC_HAES1
AccessioniPrimary (citable) accession number: Q0I513
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 3, 2006
Last modified: November 30, 2016
This is version 75 of the entry and version 1 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.