Reviewed, UniProtKB/Swiss-Prot P13670 (CHB_VIBHA)

Names and origin

Protein names

Recommended name:
    N,N'-diacetylchitobiase
      Short name=Chitobiase
    EC=3.2.1.52
Alternative name(s):
    N-acetyl-beta-glucosaminidase
    Beta-N-acetylhexosaminidase

Gene names

Name:

chb

Organism

Vibrio harveyi

Taxonomic identifier

669 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	883 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolysis of terminal, non-reducing N-acetyl-beta-D-glucosamine residues in chitobiose and higher analogs, and in glycoproteins.
Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Pathway	Glycan degradation; chitin degradation.
Subcellular location	Cell outer membrane; Lipid-anchor.
Induction	By chitobiose.
Post-translational modification	This protein is probably a lipoprotein, its processing is inhibited by globomycin.
Sequence similarities	Belongs to the glycosyl hydrolase 20 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Lipoprotein Palmitate
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell outer membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17
	Chain	18 – 883	866	N,N'-diacetylchitobiase		PRO_0000012019
Sites
	Active site	537	1	Proton donor By similarity
Amino acid modifications
	Lipidation	18	1	N-palmitoyl cysteine Probable
	Lipidation	18	1	S-diacylglycerol cysteine
	Disulfide bond	54 ↔ 64		By similarity
	Disulfide bond	394 ↔ 402		By similarity
	Disulfide bond	502 ↔ 577		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13670-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 8ED14598B1FEEBCE	FASTA	883	97,771
	10 20 30 40 50 60 MLKHSLIAAS VITTLAGCSS LQSSEQQVVN SLADNLDIQY EVLTNHGANE GLACQDMGAE 70 80 90 100 110 120 WASCNKVNMT LVNQGEAVDS KDWAIYFHSI RLILDVDNEQ FKISRVTGDL HKLEPTDKFD 130 140 150 160 170 180 GFAAGEEVVL PLVGEYWQLF ETDFMPGAFV SAPNAEPKMI ASLNTEDVAS FVTGLEGNNL 190 200 210 220 230 240 KRTPDDNNVF ANAVSRFEKN EDLATQDVST TLLPTPMHVE AGKGKVDIAD GIALPKDAFD 250 260 270 280 290 300 ATQFAAIQDR AEVVGVDVRG DLPVSITVVP ADFTGELAKS GAYEMSIKGD GIVIKAFDQA 310 320 330 340 350 360 GAFYAVQSIF GLVDSQNADS LPQLSIKDAP RFDYRGVMVD VARNFHSKDA ILATLDQMAA 370 380 390 400 410 420 YKMNKLHLHL TDDEGWRLEI PGLPELTEVG ANRCFDTQEK SCLLPQLGSG PTTDNFGSGY 430 440 450 460 470 480 FSKADYVEIL KYAKARNIEV IPEIDMPAHA RAAVVSMEAR YDRLMEEGKE AEANEYRLMD 490 500 510 520 530 540 PQDTSNVTTV QFYNKQSFIN PCMESSTRFV DKVISEVAAM HQEAGAPLTT WHFGGDEAKN 550 560 570 580 590 600 IKLGAGFQDV NAEDKVSWKG TIDLSKQDKP FAQSPQCQTL ITDGTVSDFA HLPSHFAEEV 610 620 630 640 650 660 SKIVAEKGIP NFQAWQDGLK YSDGEKAFAT ENTRVNFWDV LYWGGTSSVY EWSKKGYDVI 670 680 690 700 710 720 VSNPDYVYMD MPYEVDPKER GYYWATRATD TRKMFGFAPE NMPQNAETSV DRDGNGFTGK 730 740 750 760 770 780 GEIEAKPFYG LSAQLWSETV RNDEQYEYMV FPRVLAAAQR AWHRADWEND YKVGVEYSQN 790 800 810 820 830 840 SNLVDKASLN QDYNRFANVL GQRELAKLEK SGIDYRLPVP GAKVEDGKLA MNVQFPGVTL 850 860 870 880 QYSLDGENWL TYADNARPNV TGEVFIRSVS ATGEKVSRIT SVK

References

[1]	"N,N'-diacetylchitobiase of Vibrio harveyi. Primary structure, processing, and evolutionary relationships." Soto-Gil R.W., Zysking J.W. J. Biol. Chem. 264:14778-14783(1989) [PubMed: 2670926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J05004 Genomic DNA. Translation: AAA88682.1.
PIR	A36511.
3D structure databases
HSSP	HSSP built from PDB template 1QBA based on UniProtKB Q54468.
ModBase	Search...
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
Enzyme and pathway databases
BRENDA	3.2.1.52. 351.
Family and domain databases
InterPro	IPR004866. CB_bd_Hex_N. IPR012291. CBD_carb_bd_dom. IPR013812. Glyco_hydro_2/20_Ig-like. IPR001540. Glyco_hydro_20. IPR004867. Glyco_hydro_20_C. IPR015883. Glyco_hydro_20_cat-core. IPR013781. Glyco_hydro_sg_catalytic. IPR015882. HexNAc-like_b. [Graphical view]
Gene3D	G3DSA:2.60.40.290. CBD_carb_bd. 1 hit. G3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR22600. Glyco_hydro_20. 1 hit.
Pfam	PF03173. CHB_HEX. 1 hit. PF03174. CHB_HEX_C. 1 hit. PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view]
PRINTS	PR00738. GLHYDRLASE20.
PROSITE	PS51257. PROKAR_LIPOPROTEIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHB_VIBHA

Accession

Primary (citable) accession number: P13670

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	October 13, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)