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Database: UniProt
Entry: A0A0T9XL68_SALET
LinkDB: A0A0T9XL68_SALET
Original site: A0A0T9XL68_SALET 
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
//
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