P75949 (NAGZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-hexosaminidase
EC=3.2.1.52

Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase

Gene names

Name:	nagZ
Synonyms:	ycfO
Ordered Locus Names:	b1107, JW1093

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides. HAMAP-Rule MF_00364
Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. HAMAP-Rule MF_00364
Enzyme regulation	Slightly inhibited by GlcNAc and N-acetylmuramic acid and strongly inhibited by N-acetylglucosaminolactone. HAMAP-Rule MF_00364
Pathway	Cell wall biogenesis; peptidoglycan recycling. HAMAP-Rule MF_00364
Subunit structure	Monomer Potential.
Subcellular location	Cytoplasm HAMAP-Rule MF_00364.
Sequence similarities	Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 7.7. HAMAP-Rule MF_00364

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan turnover Inferred from mutant phenotype PubMed 11395446. Source: EcoliWiki regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 341	341	Beta-hexosaminidase HAMAP-Rule MF_00364		PRO_0000210785
Sites
	Active site	248	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P75949 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 9E50C8E4DA87C7A4	FASTA	341	37,595
	10 20 30 40 50 60 MGPVMLDVEG YELDAEEREI LAHPLVGGLI LFTRNYHDPA QLRELVRQIR AASRNRLVVA 70 80 90 100 110 120 VDQEGGRVQR FREGFTRLPA AQSFAALSGM EEGGKLAQEA GWLMASEMIA MDIDISFAPV 130 140 150 160 170 180 LDVGHISAAI GERSYHADPQ KALAIASRFI DGMHEAGMKT TGKHFPGHGA VTADSHKETP 190 200 210 220 230 240 CDPRPQAEIR AKDMSVFSSL IRENKLDAIM PAHVIYSDVD PRPASGSPYW LKTVLRQELG 250 260 270 280 290 300 FDGVIFSDDL SMEGAAIMGS YAERGQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV 310 320 330 340 TRLYHKGSFS RQELMDSARW KAISTRLNQL HERWQEEKAG H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli." Yem D.W., Wu H.C. J. Bacteriol. 125:324-331(1976) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.
[5]	"Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling." Cheng Q., Li H., Merdek K., Park J.T. J. Bacteriol. 182:4836-4840(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC74191.1. AP009048 Genomic DNA. Translation: BAA35914.1.
PIR	H64854.
RefSeq	NP_415625.1. NC_000913.2. YP_489375.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P75949.
SMR	P75949. Positions 1-340.
ModBase	Search...
Protein-protein interaction databases
IntAct	P75949. 8 interactions.
STRING	511145.b1107.
Protein family/group databases
CAZy	GH3. Glycoside Hydrolase Family 3.
Proteomic databases
PaxDb	P75949.
PRIDE	P75949.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74191; AAC74191; b1107. BAA35914; BAA35914; BAA35914.
GeneID	12930540. 945671.
KEGG	ecj:Y75_p1077. eco:b1107.
PATRIC	32117457. VBIEscCol129921_1151.
Organism-specific databases
EchoBASE	EB3207.
EcoGene	EG13433. nagZ.
Phylogenomic databases
eggNOG	COG1472.
HOGENOM	HOG000248526.
KO	K01207.
OMA	VVLHCNG.
ProtClustDB	PRK05337.
Enzyme and pathway databases
BioCyc	EcoCyc:G6567-MONOMER. ECOL316407:JW1093-MONOMER. MetaCyc:G6567-MONOMER.
UniPathway	UPA00544.
Gene expression databases
Genevestigator	P75949.
Family and domain databases
Gene3D	3.20.20.300. 1 hit.
HAMAP	MF_00364. NagZ.
InterPro	IPR022956. Beta_hexosaminidase_bac. IPR019800. Glyco_hydro_3_AS. IPR001764. Glyco_hydro_3_N. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00933. Glyco_hydro_3. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00775. GLYCOSYL_HYDROL_F3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAGZ_ECOLI

Accession

Primary (citable) accession number: P75949

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program