O31529 (BGAL1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-galactosidase yesZ
Short name=Beta-gal
EC=3.2.1.23

Alternative name(s):
Probable rhamnogalacturonan beta-galactosidase

Gene names

Name:	yesZ
Ordered Locus Names:	BSU07080

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in the degradation of rhamnogalacturonan derived from plant cell walls. Ref.3
Catalytic activity	Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Subunit structure	Homotrimer By similarity.
Induction	Up-regulated by growth on type I rhamnogalacturonan. Ref.3
Disruption phenotype	No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) hydrolyzation. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 42 family.
Biophysicochemical properties	Kinetic parameters: KM=3.0 mM for p-nitrophenyl beta-D-galactopyranoside (at pH 7.0 and 37 degrees Celsius) Ref.4

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	beta-galactosidase complex Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactosidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 663	663	Beta-galactosidase yesZ		PRO_0000367024
Regions
	Region	345 – 348	4	Substrate binding By similarity
Sites
	Active site	145	1	Proton donor Probable
	Active site	296	1	Nucleophile Probable
	Metal binding	110	1	Zinc By similarity
	Metal binding	153	1	Zinc By similarity
	Metal binding	155	1	Zinc By similarity
	Metal binding	158	1	Zinc By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	144	1	Substrate By similarity
Experimental info
	Mutagenesis	145	1	E → A: Hydrolysis of the covalent glycosyl-enzyme intermediate is slowed. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O31529 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 7E5799B02C0C5238	FASTA	663	74,099
	10 20 30 40 50 60 MRKLYHGACY YPELWDEETI QQDIDIMREV GVNVVRIGEF AWSVMEPEEG KIDVGFFKEI 70 80 90 100 110 120 IARLYDSGIE TIMCTPTPTP PIWFSHGRPE RMHANEKREI MGHGSRQHAC TNNPYFRKKA 130 140 150 160 170 180 AIITTAIAKE LGRLPGLIGW QLDNEFKCHV AECMCETCLR LWHDWLKNRY GVIERLNEAW 190 200 210 220 230 240 GTDVWSETYQ TFEQVPQPGP APFLHHASLR TMYQLFSMEM IASFADEQAK IIRCYSDAPI 250 260 270 280 290 300 THNGSVMFSV DNERMFQNLD FASYDTYASQ ENASAFLLNC DLWRNLKQGR PFWILETSPS 310 320 330 340 350 360 YAASLESSAY PHADGYLQAE AVSSYALGSQ GFCYWLWRQQ RSGSEISHGS VLSAWGEPTI 370 380 390 400 410 420 GYQNVLAVER ARKEIEPIIL STEPVQAEAA MTYSDRAKAF IKTEPHRGLR HRSLVTHFYE 430 440 450 460 470 480 RILNTGIHRD LIPEGAPLDG YRLLFTPFVP YLSSEFIKKA SAFAEAGGIW ITGPLTGGRT 490 500 510 520 530 540 CEHTIHTDCG LGELEKTSGI KTLFTFPMNE NVNTGKAFGI TAPLGLWSAV FDTESGNTLG 550 560 570 580 590 600 TVEAGPGAGH AFLTERNYGE GKIVMLGSLP SGKEGDAMLE ALVRHYAEEA VISSRSDVTP 610 620 630 640 650 660 GTIVAPRIGE NGLVWIVVNM DGKGGSVTLP ESGTDLLTHR LEKAGRLAVG PHEYRVIQFD NHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases." Shipkowski S., Brenchley J.E. Appl. Environ. Microbiol. 72:7730-7738(2006) [PubMed: 17056685] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[3]	"Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene clusters responsible for rhamnogalacturonan depolymerization." Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K. Appl. Environ. Microbiol. 73:3803-3813(2007) [PubMed: 17449691] [Abstract] Cited for: FUNCTION IN DEGRADATION OF TYPE I RHAMNOGALACTURONAN, INDUCTION. Strain: 168.
[4]	"Identification of the catalytic nucleophile in family 42 beta-galactosidases by intermediate trapping and peptide mapping: YesZ from Bacillus subtilis." Shaikh F.A., Muellegger J., He S., Withers S.G. FEBS Lett. 581:2441-2446(2007) [PubMed: 17485082] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF GLU-145.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL009126 Genomic DNA. Translation: CAB12527.1.
PIR	A69798.
RefSeq	NP_388589.1. NC_000964.3.
3D structure databases
ProteinModelPortal	O31529.
SMR	O31529. Positions 17-149.
ModBase	Search...
Protein family/group databases
CAZy	GH42. Glycoside Hydrolase Family 42.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000001763; EBBACP00000001763; EBBACG00000001761.
GeneID	936080.
GenomeReviews	Gene locus BSU07080 in contig AL009126_GR.
KEGG	bsu:BSU07080.
NMPDR	fig|224308.1.peg.708.
PATRIC	18973064. VBIBacSub10457_0746.
Organism-specific databases
GenoList	BSU07080.
Phylogenomic databases
GeneTree	EBGT00050000006111.
HOGENOM	HBG344844.
OMA	SDAPITH.
PhylomeDB	O31529.
ProtClustDB	CLSK537149.
Enzyme and pathway databases
BioCyc	BSUB:BSU07080-MONOMER.
Family and domain databases
InterPro	IPR013739. Beta_galactosidase_C. IPR013738. Beta_galactosidase_Trimer. IPR003476. Glyco_hydro_42. IPR013529. Glyco_hydro_42_N. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KO	K01190.
Pfam	PF02449. Glyco_hydro_42. 1 hit. PF08533. Glyco_hydro_42C. 1 hit. PF08532. Glyco_hydro_42M. 1 hit. [Graphical view]
PIRSF	PIRSF001084. B-galactosidase. 1 hit.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BGAL1_BACSU

Accession

Primary (citable) accession number: O31529

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program