ID J7T7U9_STRSL Unreviewed; 1298 AA.
AC J7T7U9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Fructan beta-fructosidase {ECO:0000313|EMBL:EJO17345.1};
DE EC=3.2.1.80 {ECO:0000313|EMBL:EJO17345.1};
GN ORFNames=RSSL_01269 {ECO:0000313|EMBL:EJO17345.1};
OS Streptococcus salivarius K12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1200793 {ECO:0000313|EMBL:EJO17345.1, ECO:0000313|Proteomes:UP000006983};
RN [1] {ECO:0000313|EMBL:EJO17345.1, ECO:0000313|Proteomes:UP000006983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Streptococcus salivarius K12
RC {ECO:0000313|Proteomes:UP000006983};
RX PubMed=23045482; DOI=10.1128/JB.01268-12;
RA Barretto C., Alvarez-Martin P., Foata F., Renault P., Berger B.;
RT "Genome Sequence of the Lantibiotic Bacteriocin Producer Streptococcus
RT salivarius Strain K12.";
RL J. Bacteriol. 194:5959-5960(2012).
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:EJO17345.1}.
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DR EMBL; ALIF01000001; EJO17345.1; -; Genomic_DNA.
DR RefSeq; WP_002891210.1; NZ_ALIF01000001.1.
DR PATRIC; fig|1200793.3.peg.1225; -.
DR Proteomes; UP000006983; 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 InterPro; IPR010496; 3-keto-disaccharide_hydrolase.
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; IPR022263; KxYKxGKxW.
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; PF06439; 3keto-disac_hyd; 2.
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 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 PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EJO17345.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EJO17345.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..1298
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003798224"
FT DOMAIN 928..1007
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT REGION 65..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1298 AA; 144842 MW; 3C0010CCE5FD848F CRC64;
MNDTVCKNWF MHKSGKTWVY GCALVSFAGL ALAGPVYADQ VEQATVSPIP QEVVAQTDYQ
VEVAPSTTKE VPQVVEPSPS LVSESAKTAQ ENPTHSKLDQ PKEEQVQASE AEKVTNQAQG
ADLNQTSQET PVETNSTSPV HVTEEKTDLP NNEAVTNLEG MTADQNGHWE MQADGIHSEA
KDKGDSFLYS KSEGKNFVYS TDVTFKEAGG AAALIFRGNN DSSNKNMYGV NVDSGNHKVK
FWRWVNNQDI QLVDEKDVTP TAGENYNLRV VAANQWLSYY VNDVLVASTG DSVLQKSDKG
QPQVLPEGYF GLLNWNANVI FKNTRYVNLD DASLPLIDNL VVTSKTGSVE KQAQFFSEEP
LHIQYVGHNA ETVGFDITKH NPNAVIKVED AKGNVYTDIS QLPVAVGANY FIIESSMTDS
LGRPVTLTYR VNIHRRQSDD VYYNELYRDQ YHYSVKDGWA NDPNGLVFYK GRYHLFYQFY
DDTKWGPMHW AHATSRDLLH WDEEPIAFYP DATGHMFSGS VVVDSTNSSG LFKSPEGGLV
AIITSNGNGQ RIEIAYSEDE GRTWQKYDKV VADWSQDPLQ NQDFRDPKVF RWNNQWFMVL
AGGPLRIYSS QDLKNWQVET TYKDLHTECP DLYPIVANDG ALKWVLSRGG RSYKVGDFKQ
VDGKWAFVAD DVYQDHDEIM NFGKDSYAAM TYYVHDFGTA DHPNIPQLTE INWMNTWEDY
CNLVADTVGQ KFNGTFNLNL DLGLVKSGDR YLLTQTPVKA YESLRDTENA QYFENVTVAS
DNELLKDFKG DTYEVVSHFV PGKDTTAVGF NLRVGDGQAT KVVYDLTKET LSIDRSQSGT
ILSDAFAKVN SQQVTRNEDG SIDLHLYVDR ASVEVFAKGN TVAGANQIFP SPRAVGASVL
VEGGPAKANI AIYPLKSTWT DKKEVTKAVA MNTTVAGHLA LEVGQSKDLQ VYLAPASEEQ
DVTWTVSDPS LVSYTEHDNK LSLKALHKGH LTVTATSVEN PSLTKTFNID ITLNNFATNL
KGLKAVTGNW YIDDDTLYDS NVSANDFFMA YESNGFKQFD YDIDVKYQHG LVNLFVAAER
EEPGRAYSVQ FADNDTVRLF RFGGETIAEA HLDRAINDGQ YHHVKVVKGK DTMTVYVNGK
EVLHHQFDAV DNYFNQAHVG VGLWDGAVEF KNFFVTEKMT NTSSDTTDEP IKPDPQPEPS
PEPNPENKPV EPEHQPEVAP EPEPTGQNNG HDSTNTVPDS SQDNTSKQEE SNTPVETPKT
VTPLVENLLK KFNAFSLSTF LANIAKETWH FLTKWLFS
//
