PTFAX_RHOCA
ID PTFAX_RHOCA Reviewed; 827 AA.
AC P23388;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Multiphosphoryl transfer protein {ECO:0000303|PubMed:2193161};
DE Short=MTP {ECO:0000303|PubMed:2193161};
DE AltName: Full=Triphosphoryl transfer protein {ECO:0000305};
DE Short=TTP {ECO:0000305};
DE Includes:
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:2193161};
DE EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE AltName: Full=Phosphotransferase system enzyme I {ECO:0000303|PubMed:2193161};
DE Includes:
DE RecName: Full=Phosphocarrier protein HPr {ECO:0000303|PubMed:2193161};
DE Short=Protein H {ECO:0000303|PubMed:2193161};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIA component {ECO:0000303|PubMed:2193161};
DE AltName: Full=EIII-Fru {ECO:0000303|PubMed:2193161};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:2193161};
GN Name=fruB(HI) {ECO:0000303|PubMed:2193161};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 938 / 37b4;
RX PubMed=2193161; DOI=10.1016/s0022-2836(05)80256-6;
RA Wu L.-F., Tomich J.M., Saier M.H. Jr.;
RT "Structure and evolution of a multidomain multiphosphoryl transfer protein.
RT Nucleotide sequence of the fruB(HI) gene in Rhodobacter capsulatus and
RT comparisons with homologous genes from other organisms.";
RL J. Mol. Biol. 213:687-703(1990).
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. The
CC enzyme II FruAB PTS system is involved in fructose transport.
CC {ECO:0000250|UniProtKB:P45597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC Evidence={ECO:0000250|UniProtKB:P08839};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08839};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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: In contrast to classical PTS systems, the fructose-specific PTS
CC has no requirement for HPr and Enzyme I; FruB combines a IIA domain
CC with an Enzyme I and a HPr domains. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; X53150; CAA37301.1; -; Genomic_DNA.
DR PIR; S10639; S10639.
DR RefSeq; WP_013068252.1; NZ_VIBE01000014.1.
DR AlphaFoldDB; P23388; -.
DR SMR; P23388; -.
DR PRIDE; P23388; -.
DR GeneID; 31491370; -.
DR OMA; EGHGVAW; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00367; PTS-HPr_like; 1.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 1.10.274.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.30.1340.10; -; 1.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR002114; PTS_HPr_Ser_P_site.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF00381; PTS-HPr; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR SUPFAM; SSF47831; SSF47831; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR SUPFAM; SSF55594; SSF55594; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR01003; PTS_HPr_family; 1.
DR TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 1.
DR PROSITE; PS00589; PTS_HPR_SER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphoprotein;
KW Phosphotransferase system; Sugar transport; Transferase; Transport.
FT CHAIN 1..827
FT /note="Multiphosphoryl transfer protein"
FT /id="PRO_0000186512"
FT DOMAIN 2..142
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417,
FT ECO:0000305|PubMed:2193161"
FT DOMAIN 157..245
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000305|PubMed:2193161"
FT REGION 270..827
FT /note="PTS EI"
FT /evidence="ECO:0000305|PubMed:2193161"
FT ACT_SITE 62
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417,
FT ECO:0000305|PubMed:2193161"
FT ACT_SITE 171
FT /note="Pros-phosphohistidine intermediate; for HPr
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000305|PubMed:2193161"
FT ACT_SITE 457
FT /note="Tele-phosphohistidine intermediate; for PTS EI
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P08839,
FT ECO:0000255|PROSITE-ProRule:PRU00417,
FT ECO:0000305|PubMed:2193161"
FT ACT_SITE 764
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 564
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT BINDING 600
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 693
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 716..717
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 717
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 727
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT MOD_RES 62
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305"
FT MOD_RES 171
FT /note="Phosphohistidine; by EI"
FT /evidence="ECO:0000305"
FT MOD_RES 457
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000305"
SQ SEQUENCE 827 AA; 86394 MW; 82E536754187696B CRC64;
MIPLTSELVA IGKTATDKAD AIAQAVDLLT AAGKIDPRYG QSMMGREAVA NTFLGNGIAI
PHGLPQDRDL IHDTAIAVVQ LPAGVEWAPG DTARLVVAIA AKSDEHLQVL SNLTDVLGDE
AEAERLATTL DAAVIVARLT GAAAPVAAPA ETPADFAQGI DVVVTGAHGL HARPATTLVD
LAKGFAAEIR IRNGAKVANG KSLISLLNLG AAQGAALRIS AEGADATAAL AAIAAAFEAG
LEDEEDTGAA APEAATPGLT GAGASMASYE GRTLVGISSS PGYALAPVFR FARDEVVFDT
DAADAAFETD RLDTALQTAW HELEELHDEV WKTSGPARAA IFRAHQEFLH DPEMVAEAKA
LIGQGRSAGF AWHRVFSDRA DMLGAMKDAV LSGRAIDLRD AGQRVLQHLG RVRTGETHLP
TAPCILLADD LTPSDTARLD PALVRGLATA QGGPTSHTSI IARALDIPAV AGVGPRLLDL
ATGTPVLLDG GAGVIVVAPT EADKARAETA MAALTAQREL EARERYKPAL TVDGARVEVV
ANISDVAEAI ASVEAGAEGV GLLRTEFLFV NREAPPGEDE QLAIYAAMLS ALNGLPIIIR
TLDVGGDKEI PYLRMPVEQN PFLGERGIRF CLSHEDLFRT QLRAIYRASA GGQVRIMFPM
IAMIEELETA RRIAEEVRLE VGAAPVEIGI MIEIPSAVMM APELAKRVDF FSIGTNDLTQ
YALAMDRMHP VLAKQADGLH PAVLRLIDST VRAAEAARIW VGACGGIAGD PVGAAVLSGL
GVRELSVSIP AVAGIKAQLR HSAMAENRDL ARRALACTTA AEVRGLK
