ID A0A1G8M3B7_9MICC Unreviewed; 681 AA.
AC A0A1G8M3B7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=SAMN04488693_11615 {ECO:0000313|EMBL:SDI62277.1};
OS Arthrobacter subterraneus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=335973 {ECO:0000313|EMBL:SDI62277.1, ECO:0000313|Proteomes:UP000199258};
RN [1] {ECO:0000313|EMBL:SDI62277.1, ECO:0000313|Proteomes:UP000199258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP_1H {ECO:0000313|EMBL:SDI62277.1,
RC ECO:0000313|Proteomes:UP000199258};
RA de Groot N.N.;
RL Submitted (OCT-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; FNDT01000016; SDI62277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8M3B7; -.
DR STRING; 335973.SAMN04488693_11615; -.
DR OrthoDB; 9782569at2; -.
DR Proteomes; UP000199258; Unassembled WGS sequence.
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:UP000199258};
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 320..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 490..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 632..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..147
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
FT DOMAIN 183..278
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 310..672
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT REGION 152..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 69304 MW; F919CC31BA4F9EBB CRC64;
MSAMITPELV VLDKSLGNDR AGVIRRLAEL VVAQGRADQV EGLFADALAR EEKTATGIPG
GIAIPHCRST AVLEPTLAMA RLEPKVDFGA KDGPADLVFF IAAPEGADQQ HLKLLSKLAR
SLIKKDFTAA LRAASSEQEI VALVEEALDA GPAKKEGGAT SVNPESADPG TTTPPVAART
KRLIAVTACP TGIAHTYMAA DSLVAAAKER GIDLQVETQG SSASTPLDPS VIAAADAVIF
AVDVDVRDKH RFAGKPVINA PVKRGIDEPG VMVEEALAAA DNPNARRVAD SSTPGTHDDE
SGSESIGGQL KRALLTGVSY MIPFVAGGGL LIALGFLLGG YDITGFADDM VVNNSLWNLP
TEFPETASGA LGAYLGAVLF KIGALSMGFL VPALAGYIAY ALADRPGIAP GFVAGAVAGF
MGAGFLGAIV GGLLAGYVAM KIGKLSVPRW LRGLMPVVII PLVASIVASG LMILILGGPI
AGLTVALNDW LSGLTGAGAL LLGVILGLMM AIDLGGPINK VAYAFAVAGL GAGTVANQAP
WQIMAAVMAA GMVPPLAMAL ATVIDRRRFS LAERENGKAA WLLGSAFISE GAIPFAAADP
LRVIPAGMLG SAVTGAIIMG TGVTSQAPHG GIFVFFAIGN VVMFVVAILV GMVISALAVV
ALKRFAVRKP VPAAASESVA A
//
