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   27-MAR-2024, entry version 160.
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; Bacillota; 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   DNASU; 1029658; -.
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   OrthoDB; 9759709at2; -.
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   CDD; cd18622; GH32_Inu-like; 1.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR025883; Cadherin-like_b_sandwich.
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   NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR   PANTHER; PTHR42800; EXOINULINASE INUD (AFU_ORTHOLOGUE AFUA_5G00480); 1.
DR   PANTHER; PTHR42800:SF1; EXOINULINASE INUD (AFU_ORTHOLOGUE AFUA_5G00480); 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF12733; Cadherin-like; 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; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 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
//