PTFAX_XANCP
ID PTFAX_XANCP Reviewed; 838 AA.
AC P45597; Q03397;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Multiphosphoryl transfer protein {ECO:0000303|PubMed:7496537};
DE Short=MTP {ECO:0000303|PubMed:7496537};
DE AltName: Full=Triphosphoryl transfer protein {ECO:0000305};
DE Short=TTP {ECO:0000305};
DE Includes:
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:7496537};
DE EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE AltName: Full=Phosphotransferase system enzyme I {ECO:0000303|PubMed:7496537};
DE Includes:
DE RecName: Full=Phosphocarrier protein HPr {ECO:0000303|PubMed:7496537};
DE Short=Protein H {ECO:0000303|PubMed:7496537};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIA component {ECO:0000303|PubMed:7496537};
DE AltName: Full=EIII-Fru {ECO:0000303|PubMed:7496537};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:7496537};
GN Name=fruB {ECO:0000303|PubMed:7496537}; OrderedLocusNames=XCC2370;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP DOMAIN.
RC STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
RX PubMed=7496537; DOI=10.1099/13500872-141-9-2253;
RA de Crecy-Lagard V., Binet M., Danchin A.;
RT "Fructose phosphotransferase system of Xanthomonas campestris pv.
RT campestris: characterization of the fruB gene.";
RL Microbiology 141:2253-2260(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 825-838.
RC STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
RX PubMed=1655739; DOI=10.1016/s0021-9258(18)55249-2;
RA de Crecy-Lagard V., Bouvet O.M., Lejeune P., Danchin A.;
RT "Fructose catabolism in Xanthomonas campestris pv. campestris. Sequence of
RT the PTS operon, characterization of the fructose-specific enzymes.";
RL J. Biol. Chem. 266:18154-18161(1991).
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:0000269|PubMed:7496537}.
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|PubMed:7496537}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow normally on glucose
CC but are unable to grow on fructose, mannose, mannitol or sucrose.
CC {ECO:0000269|PubMed:7496537}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; Z37113; CAA85482.1; -; Genomic_DNA.
DR EMBL; AE008922; AAM41648.1; -; Genomic_DNA.
DR EMBL; M69242; AAA27600.1; -; Genomic_DNA.
DR PIR; C40944; C40944.
DR PIR; S51680; S51680.
DR RefSeq; NP_637724.1; NC_003902.1.
DR RefSeq; WP_011037513.1; NC_003902.1.
DR AlphaFoldDB; P45597; -.
DR SMR; P45597; -.
DR STRING; 340.xcc-b100_1802; -.
DR EnsemblBacteria; AAM41648; AAM41648; XCC2370.
DR KEGG; xcc:XCC2370; -.
DR PATRIC; fig|190485.4.peg.2524; -.
DR eggNOG; COG1080; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_007308_4_0_6; -.
DR OMA; EGHGVAW; -.
DR Proteomes; UP000001010; Chromosome.
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; Reference proteome; Sugar transport;
KW Transferase; Transport.
FT CHAIN 1..838
FT /note="Multiphosphoryl transfer protein"
FT /id="PRO_0000186514"
FT DOMAIN 7..147
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417,
FT ECO:0000305|PubMed:7496537"
FT DOMAIN 161..253
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000305|PubMed:7496537"
FT REGION 274..838
FT /note="PTS EI"
FT /evidence="ECO:0000305|PubMed:7496537"
FT ACT_SITE 67
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 175
FT /note="Pros-phosphohistidine intermediate; for HPr
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 460
FT /note="Tele-phosphohistidine intermediate; for PTS EI
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P08839,
FT ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 768
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 567
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT BINDING 603
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 697
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 720..721
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 721
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 731
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT MOD_RES 67
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305"
FT MOD_RES 175
FT /note="Phosphohistidine; by EI"
FT /evidence="ECO:0000305"
FT MOD_RES 460
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="L -> V (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="P -> A (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="L -> Q (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 561..562
FT /note="EG -> N (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="Q -> H (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="R -> Q (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="D -> N (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="L -> S (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 634..635
FT /note="LL -> SS (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="L -> S (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="R -> A (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="D -> H (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="D -> S (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="Q -> H (in Ref. 1; CAA85482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 838 AA; 88747 MW; 78C87FDBA2E4DF42 CRC64;
MSSPSIAPVT PDLVRLRATA RDKDDAIAQA AQLLVAAGCV APGYDASMRR REGLANTFLG
HGLAIPHGVG EDRHLVRRDG IAVLQLPEGV EWNPGQTTRL VVGIAAQSDT HITLLRRLTR
LIQDPAQLEA LFTTDDPAVI VAALTGDRAP DTSAAPATDL AERFEWTIAY PSGLHARPAT
RWAETARGFS ARAQVRAGDQ AADAKSLVGL LQLGLRAGDS ITVSAKGSDA PALLKRLRAV
MDSLTAQEKA DAERAAQRRA APVIGWTPPQ AQPAIVGIGA SPGVAIGIVH RLRAAQTEVA
DQPIGLGDGG VLLHDALTRT RQQLAAIQDD TQRRLGASDA AIFKAQAELL NDTDLITRTC
QLMVEGHGVA WSWHQAVEQI ASGLAALGNP VLAGRAADLR DVGRRVLAQL DPAAAGAGLT
DLPEQPCILL AGDLSPSDTA NLDTDCVLGL ATAQGGPTSH TAILSRTLGL PALVAAGGQL
LDIEDGVTAI IDGSSGRLYI NPSELDLDAA RTHIAEQQAI REREAAQRAL PAETTDGHHI
DIGANVNLPE QVAMALTQGA EGVGLMRTEF LFLERGSTPT EDEQYQTYLA MARALDGRPL
IVRALDIGGD KQVAHLELPH EENPFLGVRG ARLLLRRPDL LEPQLRALYR AAKDGARLSI
MFPMITSVPE LISLREICAR IRAELDAPEL PIGIMIEVPA AAAQADVLAR HADFFSIGTN
DLTQYVLAID RQNPELAAEA DSLHPAVLRM IRSTIDGARK HDRWVGVCGG LAGDPFGASL
LAGLGVQELS MTPNDIPAVK ARLRGRALSA LQQLAEQALQ CETAEQVRAL EAQREGQA
