ID W0ZAA1_9MICO Unreviewed; 702 AA.
AC W0ZAA1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:CDK00291.1};
GN ORFNames=MIC448_2320012 {ECO:0000313|EMBL:CDK00291.1};
OS Microbacterium sp. C448.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDK00291.1, ECO:0000313|Proteomes:UP000028883};
RN [1] {ECO:0000313|EMBL:CDK00291.1, ECO:0000313|Proteomes:UP000028883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C448 {ECO:0000313|EMBL:CDK00291.1,
RC ECO:0000313|Proteomes:UP000028883};
RX PubMed=24526651; DOI=10.1128/genomeA.01113-13;
RA Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.;
RT "Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading
RT Microbacterium sp. Strain C448.";
RL Genome Announc. Announc.2:e01113-e01113(2014).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:CDK00291.1}.
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DR EMBL; CBVQ010000149; CDK00291.1; -; Genomic_DNA.
DR AlphaFoldDB; W0ZAA1; -.
DR STRING; 1177594.MIC448_2320012; -.
DR eggNOG; COG1299; Bacteria.
DR eggNOG; COG1445; Bacteria.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_013155_1_0_11; -.
DR Proteomes; UP000028883; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; IPR013014; PTS_EIIC_2.
DR InterPro; IPR004715; PTS_IIA_fruc.
DR InterPro; IPR003353; PTS_IIB_fruc.
DR InterPro; IPR006327; PTS_IIC_fruc.
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; 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 Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Reference proteome {ECO:0000313|Proteomes:UP000028883};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDK00291.1};
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 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..161
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
FT DOMAIN 201..296
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 331..682
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 71099 MW; 073D12E763D31E90 CRC64;
MSEAGMSAAG TPHEGPPTIT PELVSLDVDL GLDKAAVIRA LAERVAAQGR ASDAGALFDA
AWAREQTDET GLPGGIAIPH AKTAAVTVPS LAFARLAPGV DFGAEDGPAD LVFLIAAPAD
AAEAHLAVLS KLARNLMQDD FTSALRAAKT DAEVVSIVRV AIGEEDAPAP AAAPASTDAA
PIAEPAVIAP VTPEHGSRPR IVAVTACATG IAHTYMAADA LTAAGQKADV EVIVEPQGSS
GYKAIDPAII AGADAVIFAV DVDVREPQRF AGKPVIRTTV KRGIDNADAL VAEAVAAASD
PTADRVPASN ADGSTATAST NTANESVGAR IKRWLLTGVS YMIPFVAGGG LLIALGFLLA
GYEVTDFAAT VIIDNSIVDL PEGGLGQYLG SVAFMIGATS MGFLVPVLAG FIAFAIADRP
GIAPGFVAGA VAVLMGAGFI GGMVGGVLAG FIAWWIGRIP APRWLRGLMP VVIIPLVGSI
FASGLMVLLL GRPIAQLVIW LSDWLNSLTG ASAIGLGIIL GLMMCFDLGG PVNKVAYTFA
TAGLAAASTS DIYSAPYLIM GAVMCAGMVP PLAMALASTV LARRRFSQVE RENGKAAWLL
GAAFISEGAI PFAAVDPLRV IPASMLGGAV TGALSMAFGV SSLAPHGGIF VFFAINPIWG
FLIALIAGTV VAAFAVVGLK TWVRMREPVA EVAPAGAVPV AA
//
