PTF3A_MYCGE
ID PTF3A_MYCGE Reviewed; 680 AA.
AC P47308;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=PTS system fructose-specific EIIABC component {ECO:0000303|PubMed:9689210};
DE AltName: Full=EIIABC-Fru {ECO:0000303|PubMed:9689210};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIA component {ECO:0000303|PubMed:9689210};
DE AltName: Full=EII-Fru {ECO:0000303|PubMed:9689210};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:9689210};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIB component {ECO:0000303|PubMed:9689210};
DE EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=EIII-Fru {ECO:0000303|PubMed:9689210};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:9689210};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIC component {ECO:0000303|PubMed:9689210};
DE AltName: Full=Fructose permease IIC component {ECO:0000303|PubMed:9689210};
GN Name=fruA {ECO:0000303|PubMed:9689210}; OrderedLocusNames=MG062;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-253.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
RN [3]
RP FUNCTION, AND DISCUSSION OF SEQUENCE.
RX PubMed=9689210; DOI=10.1089/mcg.1996.1.151;
RA Reizer J., Paulsen I.T., Reizer A., Titgemeyer F., Saier M.H. Jr.;
RT "Novel phosphotransferase system genes revealed by bacterial genome
RT analysis: the complete complement of pts genes in Mycoplasma genitalium.";
RL Microb. Comp. Genomics 1:151-164(1996).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. This
CC system is involved in fructose transport.
CC {ECO:0000250|UniProtKB:P20966, ECO:0000305|PubMed:9689210}.
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:0000250|UniProtKB:P20966};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00427}.
CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00427}.
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DR EMBL; L43967; AAC71279.1; -; Genomic_DNA.
DR EMBL; U02138; AAD12415.1; -; Genomic_DNA.
DR PIR; H64206; H64206.
DR RefSeq; WP_010869312.1; NC_000908.2.
DR AlphaFoldDB; P47308; -.
DR SMR; P47308; -.
DR STRING; 243273.MG_062; -.
DR EnsemblBacteria; AAC71279; AAC71279; MG_062.
DR KEGG; mge:MG_062; -.
DR eggNOG; COG1299; Bacteria.
DR eggNOG; COG1445; Bacteria.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_013155_1_0_14; -.
DR OMA; CKLMAPH; -.
DR OrthoDB; 1810962at2; -.
DR BioCyc; MGEN243273:G1GJ2-66-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR CDD; cd05569; PTS_IIB_fructose; 1.
DR Gene3D; 3.40.930.10; -; 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 Pfam; PF00359; PTS_EIIA_2; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00829; FRU; 1.
DR TIGRFAMs; TIGR00848; fruA; 1.
DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 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 3: Inferred from homology;
KW Cell membrane; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..680
FT /note="PTS system fructose-specific EIIABC component"
FT /id="PRO_0000186510"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 4..149
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT DOMAIN 168..264
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 298..675
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT ACT_SITE 68
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 174
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000305"
FT MOD_RES 68
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305"
FT MOD_RES 174
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ SEQUENCE 680 AA; 74090 MW; A6AC1B1D7AAA9DA4 CRC64;
MFKNLLRPSL FFNWSQKTFK NKFSFLKQAA NALQKQAVIN DNNVAFEALK KREEEITTGI
ITSLALPHLQ SQSVIEPFVA VFKVKNLDWQ SLDQKPVKLI FLIGVLVDKT NLHLDFISNF
SKLMLNETFA SKVLNVTSYN GLIKLIDLFN QQKVQDQPAV ETKKEYDFVA VTACPTGIAH
TFMAKEALEA FAKKHNLYVK VETQGTDGIQ NQLTSDDINN AKGVILACDR LIDFSRFYAN
KNVIEVSTTK AIKKPDEVYE LIKNQKGKQL ANSAKPTNQT QLAESEGEFN FNNFHKRIYR
AILSGVSYML PFVVFGGILI ALSFLIDINN ANNAGGNFGT INPVANWLNK LGGISFSLIV
PILSAYIAYA LVSRQGLLPG FVVGLISSGQ FLLNIVLTNG TIEWLAPSQV SSGFFGAIFG
GLLSACLIIV QQNYIYKKLP QSLQGIKNIL FIPLFGTLFT AGLFWVINIP LIYLNYGLSL
FLNIMNSPIL APLLGFVIGL MMCFDLGGPI NKAAYVFGVV SLQNQNAGTI SMAAAMLSGM
VPPLSIALAA SIRKSCFDKQ ELPAAYACYL MGLSFISEGA IPFVVKKPKV MLTANLIAGA
ICGALTGAFA LSIRAPHGGV FVFALLKTTL QGIEGATLQT GVGIGLALVC LIISMIVGSS
IIIGYDLIAK HNQRKQNLNS
