RHGT1_BACSU
ID RHGT1_BACSU Reviewed; 232 AA.
AC O31523;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Rhamnogalacturonan acetylesterase RhgT;
DE Short=RGAE;
DE EC=3.1.1.-;
GN Name=rhgT; Synonyms=yesT; OrderedLocusNames=BSU07020;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP INDUCTION, AND FUNCTION.
RC STRAIN=168;
RX PubMed=17449691; DOI=10.1128/aem.00147-07;
RA Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.;
RT "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene
RT clusters responsible for rhamnogalacturonan depolymerization.";
RL Appl. Environ. Microbiol. 73:3803-3813(2007).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RC STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX PubMed=17957779; DOI=10.1002/prot.21705;
RA Martinez-Martinez I., Navarro-Fernandez J., Daniel Lozada-Ramirez J.,
RA Garcia-Carmona F., Sanchez-Ferrer A.;
RT "YesT: a new rhamnogalacturonan acetyl esterase from Bacillus subtilis.";
RL Proteins 71:379-388(2008).
CC -!- FUNCTION: May play a role in the degradation of type I
CC rhamnogalacturonan derived from plant cell walls. This enzyme has a
CC broad substrate specificity, and shows strong preference for glucose
CC pentaacetate, beta-naphthylacetate, and p-nitrophenyl acetate (pNPA).
CC Also active toward acetylated xylan. {ECO:0000269|PubMed:17449691}.
CC -!- ACTIVITY REGULATION: Almost completely inhibited by
CC diethylpyrocarbonate at 5 mM and completely inhibited by
CC phenylmethylsulfonyl fluoride (PMSF) at 50 mM. Dimethyl phosphite
CC achieves only a 53% inhibition. Also inhibited by metal ions
CC (magnesium, manganese and calcium) and chelating agent (EDTA) at the
CC same level. {ECO:0000269|PubMed:17957779}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for alpha-naphthyl acetate (at 37 degrees Celsius and pH
CC 7.3) {ECO:0000269|PubMed:17957779};
CC KM=1.1 mM for beta-naphthyl acetate (at 37 degrees Celsius and pH
CC 7.3) {ECO:0000269|PubMed:17957779};
CC KM=2.8 mM for p-nitrophenyl acetate (at 37 degrees Celsius and pH
CC 7.3) {ECO:0000269|PubMed:17957779};
CC KM=7.1 mM for cephalosporin C (at 37 degrees Celsius and pH 7.3)
CC {ECO:0000269|PubMed:17957779};
CC KM=9.1 mM for glucose pentaacetate (at 37 degrees Celsius and pH 7.3)
CC {ECO:0000269|PubMed:17957779};
CC KM=124.3 mM for 7-aminocephalosporanic acid (at 37 degrees Celsius
CC and pH 7.3) {ECO:0000269|PubMed:17957779};
CC Vmax=709 umol/min/mg enzyme with alpha-naphthyl acetate (at 37
CC degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779};
CC Vmax=1163 umol/min/mg enzyme with cephalosporin C (at 37 degrees
CC Celsius and pH 7.3) {ECO:0000269|PubMed:17957779};
CC Vmax=3917 umol/min/mg enzyme with beta-naphthyl acetate (at 37
CC degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779};
CC Vmax=4360 umol/min/mg enzyme with 7-aminocephalosporanic acid (at 37
CC degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779};
CC Vmax=5160 umol/min/mg enzyme with p-nitrophenyl acetate (at 37
CC degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779};
CC Vmax=13726 umol/min/mg enzyme with glucose pentaacetate (at 37
CC degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779};
CC pH dependence:
CC Optimum pH is 8.5. The enzyme is more active in the 7.5-9.0 range,
CC achieving a sharp decrease in the activity below pH 7.0.
CC {ECO:0000269|PubMed:17957779};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. The enzyme is quite
CC thermostable in the range of 35 to 40 degrees Celsius, and suffering
CC a decrease in thermostability above 45 degrees Celsius.
CC {ECO:0000269|PubMed:17957779};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17957779}.
CC -!- INDUCTION: Up-regulated by growth on type I rhamnogalacturonan.
CC {ECO:0000269|PubMed:17449691}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB12521.1; -; Genomic_DNA.
DR PIR; C69797; C69797.
DR RefSeq; NP_388583.1; NC_000964.3.
DR RefSeq; WP_003233825.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31523; -.
DR SMR; O31523; -.
DR STRING; 224308.BSU07020; -.
DR PaxDb; O31523; -.
DR PRIDE; O31523; -.
DR EnsemblBacteria; CAB12521; CAB12521; BSU_07020.
DR GeneID; 936074; -.
DR KEGG; bsu:BSU07020; -.
DR PATRIC; fig|224308.43.peg.740; -.
DR eggNOG; COG2755; Bacteria.
DR InParanoid; O31523; -.
DR OMA; ETGWGMA; -.
DR PhylomeDB; O31523; -.
DR BioCyc; BSUB:BSU07020-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd01821; Rhamnogalacturan_acetylesterase_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR037459; RhgT-like.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR43695; PTHR43695; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..232
FT /note="Rhamnogalacturonan acetylesterase RhgT"
FT /id="PRO_0000360863"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /evidence="ECO:0000250"
SQ SEQUENCE 232 AA; 25944 MW; 0E0D893B2C9D2282 CRC64;
MMKKPIQVFL AGDSTVSDCP PHEAPMAGWG QVFGQLFSEG VLVRNHAKGG ASTNSFVEEG
RLQAIAEHIT QGDYLLIQFG HNDQKPRGTK PYSTFQQFLT LFADTAREKG AHPVFVTSVQ
RRRFDENGRI EHTLGEYPDA MKALAKELDV PVIDLLAKTK VLYEAYGPEE SKRLFVWFQP
NEHPNYPDGI EDNTHFSEKG AMEVAKLVAE GIEELGLPLK DHLVSREGKE HV
