ID F0IK30_STRSA Unreviewed; 1408 AA.
AC F0IK30;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Fructan beta-fructosidase {ECO:0000313|EMBL:EGD37451.1};
DE EC=3.2.1.80 {ECO:0000313|EMBL:EGD37451.1};
GN ORFNames=HMPREF9383_0482 {ECO:0000313|EMBL:EGD37451.1};
OS Streptococcus sanguinis SK150.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888811 {ECO:0000313|EMBL:EGD37451.1, ECO:0000313|Proteomes:UP000003530};
RN [1] {ECO:0000313|EMBL:EGD37451.1, ECO:0000313|Proteomes:UP000003530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK150 {ECO:0000313|EMBL:EGD37451.1,
RC ECO:0000313|Proteomes:UP000003530};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGD37451.1}.
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DR EMBL; AEXY01000004; EGD37451.1; -; Genomic_DNA.
DR RefSeq; WP_002908726.1; NZ_GL872442.1.
DR PATRIC; fig|888811.3.peg.478; -.
DR HOGENOM; CLU_005855_0_0_9; -.
DR Proteomes; UP000003530; Unassembled WGS sequence.
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 Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR025883; Cadherin-like_b_sandwich.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011098; G5_dom.
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 NCBIfam; TIGR01167; LPXTG_anchor; 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; PF07501; G5; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00635; BID_2; 1.
DR SMART; SM01208; G5; 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; PS51109; G5; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EGD37451.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGD37451.1};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1262..1337
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT DOMAIN 1376..1408
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 53..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1207..1244
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 54..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1408 AA; 156363 MW; 9E0362BF4EA06539 CRC64;
MKNHQEKVCK NWFMRKSGKR WVFGCALLTF GAFLLDGGGV VYADEAKANP APAQVLQADS
SAVSEPESGQ TAAPTMNADK TENLVAGETA ATVATEAGGQ DAVVESANQK ADKEDQVTAN
AKETKQEEDE QPAAKEVASE KIPAVETVDK QSGFNTNLAE AKGDKNGVWE VREQGLYSDA
RGKGDSFFYS QSQGKDFVYS TDVTFLSKEG AAALIFRSNN NPDDKSSYAV NIDGGSNNVK
FWRWQGGRDY QFINEKNIEP TDDNKYRLKV VSIGSWVSYY VNDILVASSG DYTLQRDDKG
QNTYLSEGYF GLLNWNSELL FQNTFYKEIT PQSNPELEDI RVTSSVGKVE QKGQFTAPIT
IQYVKHDAET VDLTVVAKNP AAKVSVTDAA GRVYSDLKNI PLAVGANYLT VTSTVTDADG
QEVSLTYRLN VHRRQADEIY YNELYRGQYH YSVKDGWAND PNGLVYYKGV YHFFYQFYDD
TKWGPMHWGH ATSKDLIHWE EQPIAFYPDA NGAMFSGSIV ADTTNSSGLF DNDQGGLVAL
ITADGNGQRI KLAYSKDEGR TWTKLDQIAA DWTDDPLQSQ DFRDPKVFRW EGKWFMVVAG
GPLRIYSSDN LRNWKVESTY ADLHTECPDL YPLLADDGSL KWVLSRGGRS YKVGDFRQVE
GKWTFVPDAE FALADQVMNF GKDSYAAMTY YVQDFGSKAN PTLPDIIASN WMNTWEDYCN
LVADTVGQKF NGTFNLNLKL GLIKQDRSYR LTQTPITAYQ SLRQEDKAVL YKDVEVSEKN
ELLKDFSGDQ YEIVSTFRPS ETTKKVGFNL RVGDGEVTRV TYDLEKETLS IDRSQSGILL
SNKFPQVDSQ SVKRNADGSI DLHLYVDRSS LEVFAKGYTV AGANQIFPAP NSLAARVFVE
GGAAKADIAL YPLKGIWKDK QAVTKPLELV QASPVTNNIY VGDTLDLKAY VMPASVSQAV
SWSVDQPDLV SVAEDGNKLR VTALQRGVVK VTATSKENPS LSKAFTINIS RNDFKTNVPD
LKAVSGKWYV DGESLYNQNT SANDYYMGGQ KIPFSEYNLD VDLKYQKGLI NIFYASENVD
PRNAYSIQFG DNDKIRFYHF MGETIAESSM NGKHLNDGQF HHVKLVKTKN GVSVSVDGVE
YLNHQFDTVE PYYNDAYVGL GLWDGDLEAR NFFVTNLHAP AVNKASLQKV VDSTVSLDPS
LYTDETVQAY QSALARAQSL LADEKAEQAD LDRAEQDLKT ALAALAVKPS HQVTPEEGIK
DLVEEKPFLE VIMEEIAYQT REQENPELEQ GQRRILVAGQ KGQKRVFVEV LNGQRTVLGQ
EVFSLAVDEL VEVGSKVVAE SAKQPLTRTQ PQALKQGEEG KVISSPRLQP APDSALPKTG
TQEDKFLPLA GLAFLGMGLL AGRKKQED
//
