FRUA_STRMU
ID FRUA_STRMU Reviewed; 1423 AA.
AC Q03174;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Fructan beta-fructosidase;
DE EC=3.2.1.80;
DE AltName: Full=Exo-beta-D-fructosidase;
DE AltName: Full=Fructanase;
DE Flags: Precursor;
GN Name=fruA; OrderedLocusNames=SMU_78;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5;
RX PubMed=1398976; DOI=10.1128/iai.60.11.4621-4632.1992;
RA Burne R.A., Penders J.E.C.;
RT "Characterization of the Streptococcus mutans GS-5 fruA gene encoding exo-
RT beta-D-fructosidase.";
RL Infect. Immun. 60:4621-4632(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: This protein is a fructanase enzyme which degrades levans and
CC inulins to fructose and also cleaves sucrose into glucose and fructose
CC and can therefore function as an extracellular invertase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked
CC beta-D-fructofuranose residues in fructans.; EC=3.2.1.80;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-
CC anchor {ECO:0000305}.
CC -!- INDUCTION: By sucrose, fructan substrates and fructose.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; U78296; AAA26889.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN57863.1; -; Genomic_DNA.
DR PIR; A49206; A49206.
DR RefSeq; NP_720557.1; NC_004350.2.
DR RefSeq; WP_002263413.1; NC_004350.2.
DR AlphaFoldDB; Q03174; -.
DR SMR; Q03174; -.
DR STRING; 210007.SMU_78; -.
DR CAZy; CBM66; Carbohydrate-Binding Module Family 66.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PRIDE; Q03174; -.
DR DNASU; 1029658; -.
DR EnsemblBacteria; AAN57863; AAN57863; SMU_78.
DR KEGG; smu:SMU_78; -.
DR PATRIC; fig|210007.7.peg.67; -.
DR eggNOG; COG1621; Bacteria.
DR eggNOG; COG3583; Bacteria.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_005855_0_0_9; -.
DR OMA; FYDDTKW; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0051669; F:fructan beta-fructosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR003343; Big_2.
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; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR022263; KxYKxGKxW.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR019931; LPXTG_anchor.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00635; BID_2; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49373; SSF49373; 1.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF75005; SSF75005; 1.
DR TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 2: Evidence at transcript level;
KW Cell wall; Glycosidase; Hydrolase; Peptidoglycan-anchor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..1391
FT /note="Fructan beta-fructosidase"
FT /id="PRO_0000033406"
FT PROPEP 1392..1423
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000033407"
FT DOMAIN 924..1002
FT /note="BIG2"
FT /evidence="ECO:0000255"
FT REGION 44..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..871
FT /note="Involved in binding of sugars with beta-(2,6)
FT linkages or binding of molecular weight fructans"
FT /evidence="ECO:0000250"
FT REGION 1368..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1388..1392
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 44..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 455..458
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 513..514
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 581..582
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 783
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1391
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 78
FT /note="G -> E (in Ref. 1; AAA26889)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="I -> V (in Ref. 1; AAA26889)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="S -> T (in Ref. 1; AAA26889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="T -> I (in Ref. 1; AAA26889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1290
FT /note="N -> S (in Ref. 1; AAA26889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1384
FT /note="P -> S (in Ref. 1; AAA26889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1416
FT /note="G -> S (in Ref. 1; AAA26889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1421
FT /note="R -> S (in Ref. 1; AAA26889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1423 AA; 158660 MW; 03FF85E42535ABCA CRC64;
MEEETVCKNW FMRKSGKSWI FGCAVFFVLG LATALPVAAE EISQTTAADT AVTEVRTEDS
SQTSSQETAV TETTQSEGTA SKQLTTPAVA DQTTEPTDNE PISSSDGASS PYQVTDTTEP
QQTLTPADSE PQAKADVQQA AAPKKEEINP VTNLEDMSHD TNGTWEVRED GIHSNAIGKG
DSFLYSQSSG KNFVYATDVT FKQNSGAAAL VFRSNNDSNN KNMYAVNVDI GGHKAKFWRW
VDNKDIQLID ERDVVPTADN RYTLKVVAVN NWISYYVNDI LMASTGDYVL QKADKGQNTV
IPEGHFGLLN WNGDMVFQNT KFALLDDTTA PLIDNITVRS DRGNVEKQGQ FFSEEPLHIQ
YVSNDASQVS LDIAKHNPAA TVTVEDKTGR VYTDPSHLPV NVGANYFTVK STVIDSFGRT
VTLTYRINVH RRQNDEVYYN ELYRDQYHYS VKDGWANDPN GLVYYNGVYH LFHQFYDDTK
WGPMHWAHAT STDLIHWKEE PIAFYPDSNG YMFSGCVVVD EHNSSGLFKT AKGGLVAIIT
ANGNGQRMEL AYSEDEGKTW QKYDRIVADW SNDPLQNQDF RDPKVFHWNN QWFMVLAGGP
LRIYSSNNLK DWKVESTYPD LHTECPDMYP IVANDGVLKW VLSRGGRFYK VGDFKQVDGK
WTFIADDAYK DKDQVMNFGK DSYAAMTYYV HDFGTETRPT IPKLTEVNWM NTWEDYCNLV
ADTVGQDFNG TFNLNLDLGL INENGQYILT QTPVKAYDSL RDVNTALHFK DVTVDANNTL
LKDFKGDSYE IVSHFRPDEK TTKVGFNLRV GNGQATKVIY DLQTETLSID RSQSGTILSA
AFAKVNSQHV TKNADGSIDL HIYVDRASVE VFSKNNTVAG ANQIFPNPEA VGASIIVEGG
KAQADISVYQ MKTIWTDKKD TAKPVAMNTT TAKELALQVG QSQDLQVYLA PASVRQDVEW
TISDPSLVRT SQKGNVLHLT AVKKGKLTIT AISKENPSLS KTFTISITLN NFKTNLKGLQ
SVTGKWYVDD ETLYDSNTSS NDYYMASQKP GFKEYDYDID LKYQRGLINL FVASGNIDPS
QAYSVQFGDS ETVRLYRFAG DTIAEANMGK RINDDQYHHI KVTKTKNSII ISVDGQEVMS
HNFDQVDSYF NDAYVGLGLW DGAVEFQNFF VTDHATTPKP DSDPTPQPDA PEALAQEREL
IDPATGVRVI LQKGELASIV RVKVSHIETN DAHTPAVLNA KDYDLFNITP IDKNEKVVAI
TKPATVLLPI DAGKVVDKVV YLPNTDKEEN LPFTIVSLTD SNGKKQSYVR FTAEHFSEYG
LVYQAENQTN LKSKEKQDNV AISYPLNLEQ EVKVSSISRK YAANKTADVN SVQQTEPSVM
SSSPKATLPD TGDHKTDLSQ LGVLAMIGSF LVEIAGYFKK RKD
