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Protein

Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase

Gene

icaB

Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. In fact, the IcaB deacetylase converts 15 to 20% of the GlcNAc residues of PNAG to glucosamine. N-deacetylation is crucial for attachment of the polysaccharide to the bacterial cell surface; it leads to the introduction of positive charges in the otherwise neutral PIA polymer, allowing electrostatic interactions. Deacetylation of the polymer is also essential for key virulence mechanisms of S.epidermidis, namely biofilm formation, colonization, and resistance to neutrophil phagocytosis and human antibacterial peptides (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase (EC:3.5.1.-)
Short name:
PNAG N-deacetylase
Short name:
Poly-beta-1,6-GlcNAc N-deacetylase
Alternative name(s):
Biofilm polysaccharide intercellular adhesin deacetylase
Short name:
Biofilm PIA deacetylase
Intercellular adhesion protein B
Gene namesi
Name:icaB
Ordered Locus Names:SERP2295
OrganismiStaphylococcus epidermidis (strain ATCC 35984 / RP62A)
Taxonomic identifieri176279 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000531 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Disruption phenotypei

Complete loss of the intercellular adhesion phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000002484131 – 289Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylaseAdd BLAST259

Proteomic databases

PRIDEiQ5HKP8.

Interactioni

Protein-protein interaction databases

STRINGi176279.SERP2295.

Structurei

3D structure databases

ProteinModelPortaliQ5HKP8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini113 – 289NodB homologyPROSITE-ProRule annotationAdd BLAST177

Sequence similaritiesi

Belongs to the polysaccharide deacetylase family.Curated
Contains 1 NodB homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107UVV. Bacteria.
COG0726. LUCA.
HOGENOMiHOG000280325.
OMAiLYHRFGP.

Family and domain databases

Gene3Di3.20.20.370. 1 hit.
InterProiIPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. NODB_dom.
IPR023872. PNAG_deacetylase.
[Graphical view]
PfamiPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMiSSF88713. SSF88713. 1 hit.
TIGRFAMsiTIGR03933. PIA_icaB. 1 hit.
PROSITEiPS51677. NODB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5HKP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPFKLIFIS ALMILIMTNA TPISHLNAQA NEENKKLKYE KNSALALNYH
60 70 80 90 100
RVRKKDPLND FISLLSGSKE IKNYSVTDQE FKSQIQWLKA HDAKFLTLKE
110 120 130 140 150
FIKYKEKGKF PKRSVWINFD DMDQTIYDNA FPVLKKYHIP ATGFLITNHI
160 170 180 190 200
GSTNFHNLNL LSKKQLDEMY ETGLWDFESH THDLHALKKG NKSKFLDSSQ
210 220 230 240 250
SVASKDIKKS EHYLNKNYPK NERALAYPYG LINDDKIKAM KKNGIQYGFT
260 270 280
LQEKAVTPDA DNYRIPRILV SNDAFETLIK EWDGFDEEK
Length:289
Mass (Da):33,636
Last modified:February 15, 2005 - v1
Checksum:iBED61A9BC151CE3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43366 Genomic DNA. Translation: AAC06118.1.
CP000029 Genomic DNA. Translation: AAW53184.1.
PIRiS77609.
RefSeqiWP_002484506.1. NC_002976.3.

Genome annotation databases

EnsemblBacteriaiAAW53184; AAW53184; SERP2295.
KEGGiser:SERP2295.
PATRICi19615485. VBIStaEpi130894_2230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43366 Genomic DNA. Translation: AAC06118.1.
CP000029 Genomic DNA. Translation: AAW53184.1.
PIRiS77609.
RefSeqiWP_002484506.1. NC_002976.3.

3D structure databases

ProteinModelPortaliQ5HKP8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi176279.SERP2295.

Proteomic databases

PRIDEiQ5HKP8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW53184; AAW53184; SERP2295.
KEGGiser:SERP2295.
PATRICi19615485. VBIStaEpi130894_2230.

Phylogenomic databases

eggNOGiENOG4107UVV. Bacteria.
COG0726. LUCA.
HOGENOMiHOG000280325.
OMAiLYHRFGP.

Family and domain databases

Gene3Di3.20.20.370. 1 hit.
InterProiIPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. NODB_dom.
IPR023872. PNAG_deacetylase.
[Graphical view]
PfamiPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMiSSF88713. SSF88713. 1 hit.
TIGRFAMsiTIGR03933. PIA_icaB. 1 hit.
PROSITEiPS51677. NODB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiICAB_STAEQ
AccessioniPrimary (citable) accession number: Q5HKP8
Secondary accession number(s): Q54067
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: February 15, 2005
Last modified: November 2, 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, 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.