ID A0A0T9XL68_SALET Unreviewed; 575 AA.
AC A0A0T9XL68;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000256|ARBA:ARBA00016544, ECO:0000256|PIRNR:PIRNR000732};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232, ECO:0000256|PIRNR:PIRNR000732};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000256|ARBA:ARBA00033235, ECO:0000256|PIRNR:PIRNR000732};
GN Name=ptsI {ECO:0000313|EMBL:SUE46636.1};
GN ORFNames=B7N00_11430 {ECO:0000313|EMBL:EDG5017560.1}, B7N01_20755
GN {ECO:0000313|EMBL:EDG4996844.1}, B7N35_19040
GN {ECO:0000313|EMBL:EDG5128123.1}, B7N72_15660
GN {ECO:0000313|EMBL:EDG5371539.1}, B7N78_19655
GN {ECO:0000313|EMBL:EDG5281980.1}, B7N80_15130
GN {ECO:0000313|EMBL:EDG5289713.1}, B7N84_20140
GN {ECO:0000313|EMBL:EDG5268645.1}, DRU31_19255
GN {ECO:0000313|EMBL:EBS2454422.1}, E0916_19725
GN {ECO:0000313|EMBL:ECF1448168.1}, EJV93_08940
GN {ECO:0000313|EMBL:ECA2721330.1}, ERS008198_03335
GN {ECO:0000313|EMBL:CNU68921.1}, ERS008207_03012
GN {ECO:0000313|EMBL:CNU57495.1}, EWC73_00905
GN {ECO:0000313|EMBL:ECE8534792.1}, G0B02_10370
GN {ECO:0000313|EMBL:HAC6379515.1}, G0D18_09955
GN {ECO:0000313|EMBL:HAC6680977.1}, G2206_20730
GN {ECO:0000313|EMBL:HAE0437166.1}, NCTC5754_01482
GN {ECO:0000313|EMBL:SUE46636.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE46636.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|Proteomes:UP000041314, ECO:0000313|Proteomes:UP000042394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1104 {ECO:0000313|EMBL:CNU68921.1,
RC ECO:0000313|Proteomes:UP000041314}, and D4891
RC {ECO:0000313|EMBL:CNU57495.1, ECO:0000313|Proteomes:UP000042394};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAC6379515.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6379515.1}, M123
RC {ECO:0000313|EMBL:HAC6680977.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0437166.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:SUE46636.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE46636.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EBS2454422.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136768 {ECO:0000313|EMBL:EDG4996844.1}, 138330
RC {ECO:0000313|EMBL:EDG5289713.1}, 143652
RC {ECO:0000313|EMBL:EDG5371539.1}, 273631
RC {ECO:0000313|EMBL:EDG5017560.1}, 330535
RC {ECO:0000313|EMBL:EDG5268645.1}, 333944
RC {ECO:0000313|EMBL:EDG5281980.1}, 337042
RC {ECO:0000313|EMBL:EDG5128123.1}, 387147
RC {ECO:0000313|EMBL:EBS2454422.1}, 470200
RC {ECO:0000313|EMBL:ECE8534792.1}, 598023
RC {ECO:0000313|EMBL:ECA2721330.1}, and 692616
RC {ECO:0000313|EMBL:ECF1448168.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:HAE0437166.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6379515.1}, M123
RC {ECO:0000313|EMBL:HAC6680977.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0437166.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: General (non sugar-specific) component of the
CC phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar
CC PTS). This major carbohydrate active-transport system catalyzes the
CC phosphorylation of incoming sugar substrates concomitantly with their
CC translocation across the cell membrane. Enzyme I transfers the
CC phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl
CC carrier protein (HPr). {ECO:0000256|PIRNR:PIRNR000732}.
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 ECO:0000256|PIRNR:PIRNR000732};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000732, ECO:0000256|PIRSR:PIRSR000732-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR000732}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000732}.
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DR EMBL; CQPD01000031; CNU57495.1; -; Genomic_DNA.
DR EMBL; CQPA01000031; CNU68921.1; -; Genomic_DNA.
DR EMBL; AAGUWJ010000018; EBS2454422.1; -; Genomic_DNA.
DR EMBL; AAHTVM010000004; ECA2721330.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000001; ECE8534792.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000016; ECF1448168.1; -; Genomic_DNA.
DR EMBL; AAMEJW010000029; EDG4996844.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000006; EDG5017560.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000019; EDG5128123.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000015; EDG5268645.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000017; EDG5281980.1; -; Genomic_DNA.
DR EMBL; AAMEML010000016; EDG5289713.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000017; EDG5371539.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000006; HAC6379515.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000006; HAC6680977.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000030; HAE0437166.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE46636.1; -; Genomic_DNA.
DR RefSeq; WP_000623114.1; NZ_WFIN01000006.1.
DR AlphaFoldDB; A0A0T9XL68; -.
DR SMR; A0A0T9XL68; -.
DR Proteomes; UP000041314; Unassembled WGS sequence.
DR Proteomes; UP000042394; Unassembled WGS sequence.
DR Proteomes; UP000254190; Unassembled WGS sequence.
DR Proteomes; UP000839929; Unassembled WGS sequence.
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 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; 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; IPR024692; PTS_EI.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR008731; PTS_EIN.
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 PIRSF; PIRSF000732; PTS_enzyme_I; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000732};
KW Kinase {ECO:0000256|PIRNR:PIRNR000732};
KW Magnesium {ECO:0000256|PIRNR:PIRNR000732, ECO:0000256|PIRSR:PIRSR000732-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000732};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683,
KW ECO:0000256|PIRNR:PIRNR000732}; Pyruvate {ECO:0000313|EMBL:SUE46636.1};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW ECO:0000256|PIRNR:PIRNR000732};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000732};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000732}.
FT DOMAIN 3..126
FT /note="Phosphotransferase system enzyme I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05524"
FT DOMAIN 152..222
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 250..541
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 189
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT BINDING 296
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 332
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT BINDING 454..455
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT BINDING 465
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
SQ SEQUENCE 575 AA; 63369 MW; 5A87EEE702D823F0 CRC64;
MISGILASPG IAFGKALLLK EDEIVIDRKK ISADKVDQEV ERFLSGRAKA SAQLEAIKTK
AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QATALEELDD
EYLKERAADV RDIGKRLLRN ILGLAIIDLS AIQEEVILVA ADLTPSETAQ LNLQKVLGFI
TDAGGRTSHT SIMARSLELP AIVGTGSVTA QVKNGDYLIL DAVNNQVYVN PTNDVIEQLR
AVQEQVATEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL
FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAV
RIAMDRKEIL RDQVRAILRA SAFGKLRIMF PMIISVEEVR ALRKEIEIYK QELRDEGKAF
DESIEIGVMV ETPAAATIAR HLAKEVDFFS IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS
VLNLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT
NFEDAKVLAE QALAQPTTDE LMTLVNKFIE EKTIC
//