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Protein

Membrane-bound lytic murein transglycosylase C

Gene

mltC

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
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

  1. carbon-oxygen lyase activity, acting on polysaccharides Source: UniProtKB-EC
  2. hydrolase activity, acting on glycosyl bonds Source: InterPro
  3. lytic transglycosylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: UniProtKB-HAMAP
  2. cell wall organization Source: UniProtKB-KW
  3. peptidoglycan metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cell wall biogenesis/degradation

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:HI_0761
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579 Componenti: Chromosome

Subcellular locationi

Cell outer membrane UniRule annotation; Lipid-anchor UniRule annotation

GO - Cellular componenti

  1. cell outer membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515UniRule annotationAdd
BLAST
Chaini16 – 357342Membrane-bound lytic murein transglycosylase CPRO_0000032790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi16 – 161N-palmitoyl cysteineUniRule annotation
Lipidationi16 – 161S-diacylglycerol cysteineUniRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Protein-protein interaction databases

STRINGi71421.HI0761.

Structurei

3D structure databases

ProteinModelPortaliP44049.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transglycosylase Slt family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0741.
KOiK08306.
OMAiAFDILMG.
OrthoDBiEOG6Z0Q66.
PhylomeDBiP44049.

Family and domain databases

HAMAPiMF_01616. MltC.
InterProiIPR023346. Lysozyme-like_dom.
IPR023664. Murein_transglycosylaseC.
IPR024570. Murein_transglycosylaseC_N.
IPR008258. TGlycosylase-like_SLT.
IPR000189. Transglyc_AS.
[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.

P44049-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKYLLLALL PFLYACSNSS NQGINYDEAF AKDTQGLDIL TGQFSHNIDR
60 70 80 90 100
IWGVNELLVA SRKDYVKYTD SFYTRSHVSF DEGNIVIETQ QDLNRLHNAI
110 120 130 140 150
VHTLLMGADA KGIDLFASGD VPISSRPFLL GQVVDHQGQH IANQVIASNF
160 170 180 190 200
ATYLIQNKLQ TRRLQNGHTV QFVSVPMIAN HVEVRARKYL PLIRKAAQRY
210 220 230 240 250
GIDESLILGI MQTESSFNPY AISYANAIGL MQVVPHTAGR DVFAMKGKGG
260 270 280 290 300
QPSTRYLYDP ANNIDAGVSY LWILQNQYLD GITNPTSKRF AMISAYNSGA
310 320 330 340 350
GAVLRVFDND KDTAIYKINQ MYPEQVYRIL TTVHPSSQAR NYLLKVDKAQ

KKFRVRR
Length:357
Mass (Da):40,207
Last modified:October 31, 1995 - v1
Checksum:i277DCF968E7248DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22420.1.
PIRiD64013.
RefSeqiNP_438920.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22420; AAC22420; HI_0761.
GeneIDi950821.
KEGGihin:HI0761.
PATRICi20190169. VBIHaeInf48452_0800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22420.1.
PIRiD64013.
RefSeqiNP_438920.1. NC_000907.1.

3D structure databases

ProteinModelPortaliP44049.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22420; AAC22420; HI_0761.
GeneIDi950821.
KEGGihin:HI0761.
PATRICi20190169. VBIHaeInf48452_0800.

Phylogenomic databases

eggNOGiCOG0741.
KOiK08306.
OMAiAFDILMG.
OrthoDBiEOG6Z0Q66.
PhylomeDBiP44049.

Family and domain databases

HAMAPiMF_01616. MltC.
InterProiIPR023346. Lysozyme-like_dom.
IPR023664. Murein_transglycosylaseC.
IPR024570. Murein_transglycosylaseC_N.
IPR008258. TGlycosylase-like_SLT.
IPR000189. Transglyc_AS.
[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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Entry informationi

Entry nameiMLTC_HAEIN
AccessioniPrimary (citable) accession number: P44049
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: October 31, 1995
Last modified: January 6, 2015
This is version 107 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, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.