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Database: UniProt
Entry: A0A1B3SKW9_9MOLU
LinkDB: A0A1B3SKW9_9MOLU
Original site: A0A1B3SKW9_9MOLU 
ID   A0A1B3SKW9_9MOLU        Unreviewed;       792 AA.
AC   A0A1B3SKW9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=protein-N(pi)-phosphohistidine--D-fructose phosphotransferase {ECO:0000256|ARBA:ARBA00012799};
DE            EC=2.7.1.202 {ECO:0000256|ARBA:ARBA00012799};
GN   Name=fruA {ECO:0000313|EMBL:AOG60582.1};
GN   ORFNames=SHELI_v1c06310 {ECO:0000313|EMBL:AOG60582.1};
OS   Spiroplasma helicoides.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=216938 {ECO:0000313|EMBL:AOG60582.1, ECO:0000313|Proteomes:UP000094378};
RN   [1] {ECO:0000313|EMBL:AOG60582.1, ECO:0000313|Proteomes:UP000094378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TABS-2 {ECO:0000313|EMBL:AOG60582.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         fructose 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC         ChEBI:CHEBI:64837; EC=2.7.1.202;
CC         Evidence={ECO:0000256|ARBA:ARBA00001401};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP017015; AOG60582.1; -; Genomic_DNA.
DR   RefSeq; WP_069116627.1; NZ_CP017015.1.
DR   AlphaFoldDB; A0A1B3SKW9; -.
DR   STRING; 216938.SHELI_v1c06310; -.
DR   KEGG; shj:SHELI_v1c06310; -.
DR   PATRIC; fig|216938.3.peg.643; -.
DR   OrthoDB; 9782569at2; -.
DR   Proteomes; UP000094378; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR   GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   CDD; cd05569; PTS_IIB_fructose; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR004715; PTS_IIA_fruc.
DR   InterPro; IPR003353; PTS_IIB_fruc.
DR   InterPro; IPR006327; PTS_IIC_fruc.
DR   NCBIfam; TIGR00829; FRU; 1.
DR   NCBIfam; TIGR00848; fruA; 1.
DR   NCBIfam; TIGR01427; PTS_IIC_fructo; 1.
DR   PANTHER; PTHR30505; FRUCTOSE-LIKE PERMEASE; 1.
DR   PANTHER; PTHR30505:SF0; FRUCTOSE-LIKE PTS SYSTEM EIIBC COMPONENT-RELATED; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        299..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        455..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        497..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        587..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        650..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        692..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..149
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
FT   DOMAIN          163..259
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          288..720
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51104"
SQ   SEQUENCE   792 AA;  85113 MW;  FC8818390489E2C5 CRC64;
     MELKELFHKK IAFFETDLNS KDEVIDFLTS TLEKEKFIKD AKAFKDAVYK REGEGSTGIG
     DGIAIPHVLN PTVNQSAIAF CKLKNKIDWQ SLDGQPADLI FMIMTNGKDG NEHLDALANL
     SGYLIKAEVQ EGLRKAKSVD KVKELLSQPK EKREVKGDGG YDVVGITACP TGIAHTYLAA
     EKLQEYANQL GMSAKIETQG RRGVEDKLTA KDIENAKVVI LAHDKAINGM SRFNGKKVID
     TTTKDAIYNG KDLIEKFDSN PKLKTIENAK DEEDGGSGEL TLSQFKKVKD NLLAGVSRML
     PFVVAGGIVL GLGFLLDYIY TAANGMIAVA SLDDFEKYGL GNVITGYTEK NEAVHLTYKA
     FTGMAGSIDY AGQTYYSSGS FGTIWQVAHF FSGVGKIGME LMIPILAAYV CYSIVGPQGL
     MVGAVAGLMA NGDGMVYGAI GSWSGAWTRF LPKDLSGLSS GFIGALVGAY LGGLVVFGWT
     KAMKKFGKGL QGVRDIVFIP VLSLICMAVI MLAINIPLGY VMYGLQQGIT FMAEKNLMAI
     VCIIVALMMC VDMGGPINKI AYTLGTLSVG YALVKDSSSP AYEMQTMIMT AALCGGMVPP
     LGIAVSTVIF PRQWTQKAKD AAKTNWLMGA CFISEGAIPF MIEDPKRIPV SAIVGGAITG
     AVVGIFKITI TAPHGGIFVS PLTNSLLFSG DAIQKAMGVV FFFVAVLVGA VVMGVILGFW
     RLADIRNGKL VLSGTNGVKE GLEVKLAKLN AKNNQSGVAK INSKIQKYNE FEKALLIKQE
     AHKKNIESKV KK
//
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