PTF3A_MYCPN
ID PTF3A_MYCPN Reviewed; 694 AA.
AC P75039;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=PTS system fructose-specific EIIABC component {ECO:0000250|UniProtKB:P47308};
DE AltName: Full=EIIABC-Fru {ECO:0000250|UniProtKB:P47308};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIA component {ECO:0000250|UniProtKB:P47308};
DE AltName: Full=EII-Fru {ECO:0000250|UniProtKB:P47308};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P47308};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIB component {ECO:0000250|UniProtKB:P47308};
DE EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE AltName: Full=EIII-Fru {ECO:0000250|UniProtKB:P47308};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P47308};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIC component {ECO:0000250|UniProtKB:P47308};
DE AltName: Full=Fructose permease IIC component {ECO:0000250|UniProtKB:P47308};
GN Name=fruA {ECO:0000250|UniProtKB:P47308}; OrderedLocusNames=MPN_078;
GN ORFNames=MP077;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(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:0000250|UniProtKB:P47308}.
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; U00089; AAB95725.1; -; Genomic_DNA.
DR PIR; S73403; S73403.
DR RefSeq; NP_109766.1; NC_000912.1.
DR RefSeq; WP_010874435.1; NC_000912.1.
DR AlphaFoldDB; P75039; -.
DR SMR; P75039; -.
DR STRING; 272634.MPN_078; -.
DR EnsemblBacteria; AAB95725; AAB95725; MPN_078.
DR KEGG; mpn:MPN_078; -.
DR PATRIC; fig|272634.6.peg.79; -.
DR HOGENOM; CLU_013155_1_0_14; -.
DR OMA; CKLMAPH; -.
DR BioCyc; MPNE272634:G1GJ3-122-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
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..694
FT /note="PTS system fructose-specific EIIABC component"
FT /id="PRO_0000186511"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 655..675
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 179..275
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 310..687
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 185
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 185
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ SEQUENCE 694 AA; 75164 MW; 919E12BFBCC5FF6A CRC64;
MFKPLLSAEL FFNWTAKDFK DKTSFLKQAC RVLQDKNCIK EEQIALTALK EREAQITTGI
MSKLALPHMQ SATVLKPFVA VFKVNNVDWQ SLDNQPVKLI FLIGVPKDQG NLHLEFISQF
SKLMLQDEFA NKVPNIRSFN GLINLIDSFQ QTAVASQPVV NEAAAQTEEP KDTNTQYDFV
AVTACPTGIA HTFMAKEALE KFARDHNLKV KVETQGTDGI QNQLTESDLN NTKGIILACD
RLIDLTRFYG HANVVEVSTT KAIKTPQTVY DQVVKKEGKL LGNKSSDSAS QTELKETTEQ
LSFKDFHKRI YRAILSGVSY MLPFVVFGGI LIAIAFLIDI NNAGNAGKQF GSKDPIANWF
KTLGGLSFGL IVPILSAYIA FALVGRQGLL PGFIVGLISA GKFLLNIDIV TGKIDWATES
KVSSGFFGAI FGGLLAAVLI IVQQRYIYRK LPQALQGIKN ILFIPLLGTL VTAALFWVIN
IPLIYLNYGL SKFLQIMDKP YLAPLLGLVI GLMMCFDLGG PVNKAAYVFG VVSLESQNSG
TVAMASAILS GMVPPLGIAI AATIRKQCFD KEELPAAYAC YVMGLSFISE GAIPFVAKRP
KIMLAANLIG GAVCGVLTGA FALTIRAPHG GVFVFALLKT NLEGIAGNTL QIGAGVGLAL
LALIVSSFIS AGIIIGHNLL VVRKKTKQLV NTNA
