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Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Cleaves muropeptides, but not peptidoglycan.2 Publications

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.2 Publications

pH dependencei

Optimum pH is 5.8-6.2.1 Publication

Pathwayi: peptidoglycan recycling

This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei123Substrate1
Binding sitei131Substrate1
Binding sitei191Substrate1
Sitei232Important for catalytic activity1
Active sitei234Proton donor/acceptor1
Active sitei318Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciBSUB:BSU01660-MONOMER.
UniPathwayiUPA00544.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-hexosaminidase (EC:3.2.1.52)
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
N-acetylglucosaminidase
ORF1
Gene namesi
Name:nagZ
Synonyms:ybbD, yzbA
Ordered Locus Names:BSU01660
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cell membrane PROSITE-ProRule annotation; Lipid-anchor PROSITE-ProRule annotation
  • Secretedcell wall 1 Publication

  • Note: Detected in the culture supernatant, predominantly associated with cell wall-derived particulate material. A minor proportion is detected in the soluble fraction.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell wall, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi232D → G: Strongly reduces catalytic efficiency and enzyme activity. Slightly increases substrate affinity. 1 Publication1
Mutagenesisi234H → G: Strongly reduces catalytic efficiency while increasing substrate affinity. 1 Publication1
Mutagenesisi318D → N: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16PROSITE-ProRule annotationAdd BLAST16
ChainiPRO_000001178517 – 642Beta-hexosaminidaseAdd BLAST626

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi17N-palmitoyl cysteinePROSITE-ProRule annotation1
Lipidationi17S-diacylglycerol cysteinePROSITE-ProRule annotation1

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP40406.
PRIDEiP40406.

Expressioni

Inductioni

Up-regulated during the late phase of exponential growth and during stationary phase.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000943.

Structurei

Secondary structure

1642
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 40Combined sources14
Helixi44 – 50Combined sources7
Beta strandi57 – 59Combined sources3
Helixi75 – 84Combined sources10
Beta strandi87 – 90Combined sources4
Helixi93 – 95Combined sources3
Helixi99 – 112Combined sources14
Beta strandi114 – 116Combined sources3
Beta strandi119 – 122Combined sources4
Beta strandi133 – 135Combined sources3
Helixi141 – 147Combined sources7
Helixi150 – 167Combined sources18
Beta strandi186 – 188Combined sources3
Helixi189 – 191Combined sources3
Helixi197 – 213Combined sources17
Beta strandi217 – 223Combined sources7
Helixi226 – 228Combined sources3
Beta strandi230 – 232Combined sources3
Turni233 – 235Combined sources3
Beta strandi237 – 239Combined sources3
Helixi244 – 249Combined sources6
Helixi252 – 260Combined sources9
Beta strandi265 – 268Combined sources4
Turni274 – 276Combined sources3
Beta strandi280 – 282Combined sources3
Turni284 – 286Combined sources3
Beta strandi289 – 291Combined sources3
Helixi294 – 296Combined sources3
Helixi298 – 301Combined sources4
Helixi302 – 308Combined sources7
Beta strandi313 – 316Combined sources4
Helixi323 – 326Combined sources4
Helixi331 – 341Combined sources11
Beta strandi344 – 348Combined sources5
Helixi355 – 358Combined sources4
Helixi359 – 373Combined sources15
Helixi379 – 395Combined sources17
Turni396 – 401Combined sources6
Helixi407 – 417Combined sources11
Helixi421 – 434Combined sources14
Beta strandi436 – 440Combined sources5
Helixi441 – 443Combined sources3
Beta strandi454 – 461Combined sources8
Helixi462 – 477Combined sources16
Beta strandi485 – 490Combined sources6
Helixi498 – 506Combined sources9
Beta strandi508 – 514Combined sources7
Helixi535 – 537Combined sources3
Helixi538 – 552Combined sources15
Beta strandi557 – 561Combined sources5
Helixi565 – 570Combined sources6
Beta strandi575 – 579Combined sources5
Beta strandi590 – 592Combined sources3
Helixi595 – 603Combined sources9
Beta strandi620 – 622Combined sources3
Beta strandi625 – 628Combined sources4
Turni636 – 638Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BMXX-ray1.40A/B1-642[»]
3LK6X-ray2.88A/B/C/D27-642[»]
3NVDX-ray1.70A/B1-642[»]
4GYJX-ray1.65A/B18-642[»]
4GYKX-ray1.80A/B18-642[»]
ProteinModelPortaliP40406.
SMRiP40406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40406.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni221 – 222Substrate binding2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105D17. Bacteria.
COG1472. LUCA.
HOGENOMiHOG000248527.
InParanoidiP40406.
KOiK01207.
OMAiMPDFRNW.
PhylomeDBiP40406.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P40406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPVFPLILS AVLFLSCFFG ARQTEASASK RAIDANQIVN RMSLDEKLGQ
60 70 80 90 100
MLMPDFRNWQ KEGESSPQAL TKMNDEVASL VKKYQFGGII LFAENVKTTK
110 120 130 140 150
QTVQLTDDYQ KASPKIPLML SIDQEGGIVT RLGEGTNFPG NMALGAARSR
160 170 180 190 200
INAYQTGSII GKELSALGIN TDFSPVVDIN NNPDNPVIGV RSFSSNRELT
210 220 230 240 250
SRLGLYTMKG LQRQDIASAL KHFPGHGDTD VDSHYGLPLV SHGQERLREV
260 270 280 290 300
ELYPFQKAID AGADMVMTAH VQFPAFDDTT YKSKLDGSDI LVPATLSKKV
310 320 330 340 350
MTGLLRQEMG FNGVIVTDAL NMKAIADHFG QEEAVVMAVK AGVDIALMPA
360 370 380 390 400
SVTSLKEEQK FARVIQALKE AVKNGDIPEQ QINNSVERII SLKIKRGMYP
410 420 430 440 450
ARNSDSTKEK IAKAKKIVGS KQHLKAEKKL AEKAVTVLKN EQHTLPFKPK
460 470 480 490 500
KGSRILIVAP YEEQTASIEQ TIHDLIKRKK IKPVSLSKMN FASQVFKTEH
510 520 530 540 550
EKQVKEADYI ITGSYVVKND PVVNDGVIDD TISDSSKWAT VFPRAVMKAA
560 570 580 590 600
LQHNKPFVLM SLRNPYDAAN FEEAKALIAV YGFKGYANGR YLQPNIPAGV
610 620 630 640
MAIFGQAKPK GTLPVDIPSV TKPGNTLYPL GYGLNIKTGR PL
Length:642
Mass (Da):70,580
Last modified:February 1, 1995 - v1
Checksum:iDCEA93142922F13F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19954 Genomic DNA. Translation: AAA64351.1.
AB002150 Genomic DNA. Translation: BAA19499.1.
AL009126 Genomic DNA. Translation: CAB11942.1.
PIRiI39839.
RefSeqiNP_388047.1. NC_000964.3.
WP_003234975.1. NZ_JNCM01000030.1.

Genome annotation databases

EnsemblBacteriaiCAB11942; CAB11942; BSU01660.
GeneIDi938881.
KEGGibsu:BSU01660.
PATRICi18971875. VBIBacSub10457_0171.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19954 Genomic DNA. Translation: AAA64351.1.
AB002150 Genomic DNA. Translation: BAA19499.1.
AL009126 Genomic DNA. Translation: CAB11942.1.
PIRiI39839.
RefSeqiNP_388047.1. NC_000964.3.
WP_003234975.1. NZ_JNCM01000030.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BMXX-ray1.40A/B1-642[»]
3LK6X-ray2.88A/B/C/D27-642[»]
3NVDX-ray1.70A/B1-642[»]
4GYJX-ray1.65A/B18-642[»]
4GYKX-ray1.80A/B18-642[»]
ProteinModelPortaliP40406.
SMRiP40406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000943.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Proteomic databases

PaxDbiP40406.
PRIDEiP40406.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11942; CAB11942; BSU01660.
GeneIDi938881.
KEGGibsu:BSU01660.
PATRICi18971875. VBIBacSub10457_0171.

Phylogenomic databases

eggNOGiENOG4105D17. Bacteria.
COG1472. LUCA.
HOGENOMiHOG000248527.
InParanoidiP40406.
KOiK01207.
OMAiMPDFRNW.
PhylomeDBiP40406.

Enzyme and pathway databases

UniPathwayiUPA00544.
BioCyciBSUB:BSU01660-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40406.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNAGZ_BACSU
AccessioniPrimary (citable) accession number: P40406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 121 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.