ID A0A1B3SLV1_9MOLU Unreviewed; 971 AA.
AC A0A1B3SLV1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Sucrose-6-phosphate hydrolase {ECO:0000256|RuleBase:RU365015};
DE EC=3.2.1.26 {ECO:0000256|RuleBase:RU365015};
DE AltName: Full=Invertase {ECO:0000256|RuleBase:RU365015};
GN ORFNames=SHELI_v1c09310 {ECO:0000313|EMBL:AOG60880.1};
OS Spiroplasma helicoides.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=216938 {ECO:0000313|EMBL:AOG60880.1, ECO:0000313|Proteomes:UP000094378};
RN [1] {ECO:0000313|EMBL:AOG60880.1, ECO:0000313|Proteomes:UP000094378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TABS-2 {ECO:0000313|EMBL:AOG60880.1,
RC ECO:0000313|Proteomes:UP000094378};
RA Shen W.-Y., Lo W.-S., Lai Y.-C., Kuo C.-H.;
RT "Complete genome sequence of Spiroplasma helicoides TABS-2 (DSM 22551).";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Enables the bacterium to metabolize sucrose as a sole carbon
CC source. {ECO:0000256|RuleBase:RU365015}.
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:0000256|RuleBase:RU365015};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC {ECO:0000256|RuleBase:RU365015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365015}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU365015}.
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DR EMBL; CP017015; AOG60880.1; -; Genomic_DNA.
DR RefSeq; WP_069117155.1; NZ_CP017015.1.
DR AlphaFoldDB; A0A1B3SLV1; -.
DR STRING; 216938.SHELI_v1c09310; -.
DR KEGG; shj:SHELI_v1c09310; -.
DR PATRIC; fig|216938.3.peg.946; -.
DR OrthoDB; 9759709at2; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000094378; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd18623; GH32_ScrB-like; 1.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR036878; Glu_permease_IIB.
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; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR006232; Suc6P_hydrolase.
DR NCBIfam; TIGR01322; scrB_fam; 1.
DR PANTHER; PTHR43101; BETA-FRUCTOSIDASE; 1.
DR PANTHER; PTHR43101:SF1; BETA-FRUCTOSIDASE; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU365015};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU365015};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU365015};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365015};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Reference proteome {ECO:0000313|Proteomes:UP000094378};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 107..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..89
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 106..477
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT COILED 823..857
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 28
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 971 AA; 109777 MW; D39C472FEE9B7D80 CRC64;
MTKVNYKKVG EQIIGIVGKD NITSMTHCAT RLRFVVKNKD VIDKSKFEDM EIVKGTFYNG
GQFQIILGPS IVNKVYDSLM EDSTNNFEVT QTVSIPPKNK FKYAIRILAG IFIAIMPGMV
ATGLFLGLKG AILNDSVLGL FGTSVSEVPK ALNVVISVLT DTVFAFLPAL ICYSAFKTFG
GSPVMGFVIG LMLVNPLLPN AYSVADPNSG VEPIYIFGFI PLVGYQGSVI TSIFLGFIGS
KFEKVLRKKM PNALDLMFTP FLVILVTVVS GLLVFGPILH YVETGIVYVV KAIIGIPGGI
GGFFIGCLYP VTVMTGMHHL FFLIESTMLG QTGYNPLITV CAMFGFSNAA VCFAISMRVK
KRNEKVMGIG SGVTQLLGVS EPALFGVTLR YGVRPMSIMI LCSGLGGAVL SLLGIQANSY
GLAVILSPLM YLYSWYQFGM YILIGVITFA LAFTLTFIFA SPDKILKKEQ EKKEIENKLA
LNKNEWTKEQ RYRSVKGMKH IEKAYLKNRV KHSKWRHKFH IQPKYGLLND PNGFSYYNDK
YYLFYQWFPY GAVHGLKHWN LVTSKNLVKW SNKGPKLIPT LDHESHGIFS GSSIVKDNQL
YLFYTANKRD KNWERFSSQC LAIMDEKNKI TKIEKPIIKE KPVGYTNNFR DPKIFLKDNF
YYMVVGAQRE NETGCILTYK SSDLKKWDYV GELDTKFKNF GSMWECPDIT SVDNKDVLMI
SALNNKKDNL KNIHNAVYNI GKFDAEKNKY TTDQDFMPID YGFDFYAVQT TESKDKEKIL
VGWVGLPDTD YPTDDESWAN CLSIPRKLSI VNDKLYQTPV ESIFSLRKKE QKLEKELENQ
SLKLENLESK NYELICELDT NGNGESGVKF RVGEKEFTSI YLDSKNKKII LDRNNSGILF
SEKFGEIREI PYEKNKVKFD IFVDNSTVEI FINDGEYVMT SRIFPIEDSE DIEIFANKAK
AKFDITKYNL K
//
