SCRB_BACSU
ID SCRB_BACSU Reviewed; 479 AA.
AC P07819;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Sucrose-6-phosphate hydrolase;
DE Short=Sucrase;
DE EC=3.2.1.26;
DE AltName: Full=Invertase;
GN Name=sacA; OrderedLocusNames=BSU38040; ORFNames=ipa-50d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3100393; DOI=10.1016/0378-1119(86)90258-1;
RA Fouet A., Klier A., Rapoport G.;
RT "Nucleotide sequence of the sucrase gene of Bacillus subtilis.";
RL Gene 45:221-225(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [3]
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 [4]
RP SEQUENCE REVISION TO 155-156; 161-164 AND 448.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RX PubMed=3122206; DOI=10.1073/pnas.84.24.8773;
RA Fouet A., Arnaud M., Klier A., Rapoport G.;
RT "Bacillus subtilis sucrose-specific enzyme II of the phosphotransferase
RT system: expression in Escherichia coli and homology to enzymes II from
RT enteric bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8773-8777(1987).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10067};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; M15662; AAA22723.1; -; Genomic_DNA.
DR EMBL; X73124; CAA51606.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15830.2; -; Genomic_DNA.
DR EMBL; J03006; AAA22728.1; -; Genomic_DNA.
DR PIR; A25562; A25562.
DR RefSeq; NP_391683.2; NC_000964.3.
DR RefSeq; WP_010886636.1; NZ_CP053102.1.
DR AlphaFoldDB; P07819; -.
DR SMR; P07819; -.
DR STRING; 224308.BSU38040; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; P07819; -.
DR PRIDE; P07819; -.
DR EnsemblBacteria; CAB15830; CAB15830; BSU_38040.
DR GeneID; 937277; -.
DR KEGG; bsu:BSU38040; -.
DR PATRIC; fig|224308.179.peg.4118; -.
DR eggNOG; COG1621; Bacteria.
DR InParanoid; P07819; -.
DR OMA; WTEHPVA; -.
DR PhylomeDB; P07819; -.
DR BioCyc; BSUB:BSU38040-MON; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006232; Suc6P_hydrolase.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR TIGRFAMs; TIGR01322; scrB_fam; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..479
FT /note="Sucrose-6-phosphate hydrolase"
FT /id="PRO_0000169870"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 40..43
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102..103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161..162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 155..156
FT /note="GY -> AIL (in Ref. 1; AAA22723 and 2; CAA51606)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..164
FT /note="RDPK -> SRSE (in Ref. 1; AAA22723 and 2; CAA51606)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="L -> F (in Ref. 1; AAA22723 and 2; CAA51606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 54814 MW; 53D882B4772CB3CF CRC64;
MTAHDQELRR RAYEEVEKKE PIANSDPHRQ HFHIMPPVGL LNDPNGVIYW KGSYHVFFQW
QPFQTGHGAK FWGHYTTQDV VNWKREEIAL APSDWFDKNG CYSGSAVTKD DRLYLFYTGN
VRDQDGNRET YQCLAVSDDG LSFEKKGVVA RLPEGYTAHF RDPKVWEHEG TWYMVIGAQT
ENLKGQAVLF ASDNLTEWRF LGPITGAGFN GLDDFGYMWE CPDLFSLQGS DVLIVSPQGL
EADGFRYQNV YQSGYFVGRL DYNKPELKHG EFTELDQGFD FYAPQTLEDD QGRRILFAWM
AVPDQDEGSH PTIDCHWIHC MTLPRQLTLS GQKLIQQPLP ELKAMRRNEK KIHINMHGSS
GALPVEKPER TEILLEDIHT ESGFSISIRG TATFSFHKDE GIVTLERKSF DGKRTEARHC
RIKDLHTVHM FLDASSVEIF INNGEEVLSA RYFPFPGNHE VTASATGKSE MNVGIWTLM
