Reviewed, UniProtKB/Swiss-Prot O31523 (RHGT1_BACSU)

Names and origin

Protein names

Recommended name:
    Rhamnogalacturonan acetylesterase rhgT
      Short name=RGAE
    EC=3.1.1.-

Gene names

Name:	rhgT
Synonyms:	yesT
Ordered Locus Names:	BSU07020

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	232 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play role in the degradation of type I rhamnogalacturonan derived from plant cell walls. This enzyme has a broad substrate specificity, and shows strong preference for glucose pentaacetate, beta-naphthylacetate, and p-nitrophenyl acetate (pNPA). Also active toward acetylated xylan. Ref.2
Enzyme regulation	Almost completely inhibited by diethylpyrocarbonate at 5 mM and completely inhibited by phenylmethylsulfonyl fluoride (PMSF) at 50 mM. Dimethyl phosphite achieves only a 53% inhibition. Also inhibited by metal ions (magnesium, manganese and calcium) and chelating agent (EDTA) at the same level. Ref.3
Subunit structure	Monomer. Ref.3
Induction	Up-regulated by growth on type I rhamnogalacturonan. Ref.2
Sequence similarities	Belongs to the 'GDSL' lipolytic enzyme family.
biophysicochemical properties	Kinetic parameters: KM=1.0 mM for alpha-naphthyl acetate (at 37 degrees Celsius and pH 7.3) KM=1.1 mM for beta-naphthyl acetate (at 37 degrees Celsius and pH 7.3) KM=2.8 mM for p-nitrophenyl acetate (at 37 degrees Celsius and pH 7.3) KM=7.1 mM for cephalosporin C (at 37 degrees Celsius and pH 7.3) KM=9.1 mM for glucose pentaacetate (at 37 degrees Celsius and pH 7.3) KM=124.3 mM for 7-aminocephalosporanic acid (at 37 degrees Celsius and pH 7.3) Vmax=709 µmol/min/mg enzyme with alpha-naphthyl acetate (at 37 degrees Celsius and pH 7.3) Vmax=1163 µmol/min/mg enzyme with cephalosporin C (at 37 degrees Celsius and pH 7.3) Vmax=3917 µmol/min/mg enzyme with beta-naphthyl acetate (at 37 degrees Celsius and pH 7.3) Vmax=4360 µmol/min/mg enzyme with 7-aminocephalosporanic acid (at 37 degrees Celsius and pH 7.3) Vmax=5160 µmol/min/mg enzyme with p-nitrophenyl acetate (at 37 degrees Celsius and pH 7.3) Vmax=13726 µmol/min/mg enzyme with glucose pentaacetate (at 37 degrees Celsius and pH 7.3) pH dependence: Optimum pH is 8.5. The enzyme is more active in the 7.5-9.0 range, achieving a sharp decrease in the activity below pH 7.0. Temperature dependence: Optimum temperature is 35 degrees Celsius. The enzyme is quite thermostable in the range of 35 to 40 degrees Celsius, and suffering a decrease in thermostability above 45 degrees Celsius.

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 232	232	Rhamnogalacturonan acetylesterase rhgT		PRO_0000360863
Sites
	Active site	14	1	By similarity
	Active site	182	1	By similarity
	Active site	195	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O31523-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 0E0D893B2C9D2282	FASTA	232	25,944
	10 20 30 40 50 60 MMKKPIQVFL AGDSTVSDCP PHEAPMAGWG QVFGQLFSEG VLVRNHAKGG ASTNSFVEEG 70 80 90 100 110 120 RLQAIAEHIT QGDYLLIQFG HNDQKPRGTK PYSTFQQFLT LFADTAREKG AHPVFVTSVQ 130 140 150 160 170 180 RRRFDENGRI EHTLGEYPDA MKALAKELDV PVIDLLAKTK VLYEAYGPEE SKRLFVWFQP 190 200 210 220 230 NEHPNYPDGI EDNTHFSEKG AMEVAKLVAE GIEELGLPLK DHLVSREGKE HV

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]	"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: INDUCTION, FUNCTION. Strain: 168.
[3]	"YesT: a new rhamnogalacturonan acetyl esterase from Bacillus subtilis." Martinez-Martinez I., Navarro-Fernandez J., Daniel Lozada-Ramirez J., Garcia-Carmona F., Sanchez-Ferrer A. Proteins 71:379-388(2008) [PubMed: 17957779] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT. Strain: ATCC 6633 / PCI 219 / NRS 231.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL009126 Genomic DNA. Translation: CAB12521.1.
PIR	C69797.
RefSeq	NP_388583.1.
3D structure databases
HSSP	HSSP built from PDB template 1K7C based on UniProtKB Q00017.
ModBase	Search...
Genome annotation databases
GeneID	936074.
GenomeReviews	Gene locus BSU07020 in contig AL009126_GR.
KEGG	bsu:BSU07020.
NMPDR	fig|224308.1.peg.702.
Organism-specific databases
SubtiList	BG12854. rhgT. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O31523.
OMA	O31523. HEAPMAG.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU0702-MON.
Family and domain databases
InterPro	IPR013831. Esterase_SGNH_hydro-type_subgr. IPR001087. Lipase_GDSL. IPR008265. Lipase_GDSL_AS. [Graphical view]
Gene3D	G3DSA:3.40.50.1110. Esterase_SGNH_hydro-type_subgr. 1 hit.
Pfam	PF00657. Lipase_GDSL. 1 hit. [Graphical view]
PROSITE	PS01098. LIPASE_GDSL_SER. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RHGT1_BACSU

Accession

Primary (citable) accession number: O31523

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	January 1, 1998
Last modified:	May 5, 2009
This is version 43 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)