ID F6IEB9_9SPHN Unreviewed; 840 AA.
AC F6IEB9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=PP1Y_Mpl7719 {ECO:0000313|EMBL:CCA90644.1};
OS Novosphingobium sp. PP1Y.
OG Plasmid Mpl {ECO:0000313|EMBL:CCA90644.1,
OG ECO:0000313|Proteomes:UP000009242}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA90644.1, ECO:0000313|Proteomes:UP000009242};
RN [1] {ECO:0000313|EMBL:CCA90644.1, ECO:0000313|Proteomes:UP000009242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RC PLASMID=Mpl {ECO:0000313|EMBL:CCA90644.1,
RC ECO:0000313|Proteomes:UP000009242};
RX PubMed=21685292; DOI=10.1128/JB.05349-11;
RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA Paolella G., Di Donato A., Salvatore F.;
RT "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT strain PP1Y.";
RL J. Bacteriol. 193:4296-4296(2011).
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:0000256|ARBA:ARBA00000683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; FR856861; CCA90644.1; -; Genomic_DNA.
DR RefSeq; WP_013836885.1; NC_015583.1.
DR AlphaFoldDB; F6IEB9; -.
DR KEGG; npp:PP1Y_Mpl7719; -.
DR eggNOG; COG1080; Bacteria.
DR eggNOG; COG1925; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_007308_4_1_5; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000009242; Plasmid Mpl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:InterPro.
DR CDD; cd00367; PTS-HPr_like; 1.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 3.30.1340.10; HPr-like; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 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; IPR036618; PtsI_HPr-bd_sf.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01417; PTS_I_fam; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
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 PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55594; HPr-like; 1.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Plasmid {ECO:0000313|EMBL:CCA90644.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009242};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCA90644.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 8..149
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
FT DOMAIN 162..250
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 840 AA; 88685 MW; 191E0B8EC9E2AE99 CRC64;
MLADAIPASH AADLVRIDAS ATDKTDAIRQ VGQLLVAAGC VAPGYEESMV RREALANTFL
GSGVAIPHGL GEDKGLVRND GIAILQLREG IDWNPGQRAH IVVGIAANSD SHITILRRLT
RLIQDEERLQ VLIATDDPAE FSRALLEDGT PAAPSVPAED LAHTAAWIVD YPTGLHARPA
STWVEAARAS AVRLRVRHGE ESADPRNLVA LLQLGLRCGD EIKFSAEGPA AQDALEKFVA
TVRSLSAREK EDAARAAEKR KAPVRCWTPV GSPRMIAGVA ASPGLAIGPI HVLSAAELSV
PDVPVDLVNG GAMLNEALVR TRAQMKALID DTTRRLGASE AAIFKAQTEL LEDTDIITLT
CQLMVEGHGV AWSWHQAVQR IAGKLSALGN PVLAARAADL TDVGRRVLAE IDPGLVTGTL
ADLPEEPCIL VAPDLSPSDT ATLDTARVAG IATALGGPTS HSAILARTLG LPSVVASGAD
LLAAASGTTA IVDGDGGRVW LDPSEKDLAS ARGWIADLTA QRVAEEEERG QPAVTRDGHR
VEIAANVNRP DQVGFALAQG GEGVGLMRTE FLFLESGNTP GEDEQFAVYR AMIDALSAGN
EERPLIVRAL DIGGDKQVPH LELPVEENPF LGVRGARLLL RRPDLLEPQL RALYRAAREG
GNLSIMFPMI TSAHELLALR KRCEAVRAEL DAPQVPIGIM IEVPAAAVQA AQLAAHADFF
SIGTNDLTQY TLAIDRQNPE LAGEADSLHP AVLRMIAATV EGARTHDRWV GVCGGIAGDP
FGAALLVGLG VDELSMTPRD IPAVKARLRG CDRGELNRLA AQALEMDGAA QVRALDGKAM
//
