ID U7D6Y1_9BACT Unreviewed; 588 AA.
AC U7D6Y1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 ORFNames=CALK_1364 {ECO:0000313|EMBL:ERP31703.1};
OS Chitinivibrio alkaliphilus ACht1.
OC Bacteria; Fibrobacterota; Chitinivibrionia; Chitinivibrionales;
OC Chitinivibrionaceae; Chitinivibrio.
OX NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP31703.1, ECO:0000313|Proteomes:UP000017148};
RN [1] {ECO:0000313|EMBL:ERP31703.1, ECO:0000313|Proteomes:UP000017148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACht1 {ECO:0000313|EMBL:ERP31703.1,
RC ECO:0000313|Proteomes:UP000017148};
RX PubMed=24112708;
RA Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S.,
RA Muyzer G., Mardanov A.V., Ravin N.V.;
RT "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a novel
RT extremely haloalkaliphilic anaerobic chitinolytic bacterium from the
RT candidate phylum Termite Group 3.";
RL Environ. Microbiol. 0:0-0(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERP31703.1}.
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DR EMBL; ASJR01000010; ERP31703.1; -; Genomic_DNA.
DR RefSeq; WP_022636826.1; NZ_ASJR01000010.1.
DR AlphaFoldDB; U7D6Y1; -.
DR STRING; 1313304.CALK_1364; -.
DR PATRIC; fig|1313304.3.peg.1298; -.
DR eggNOG; COG1080; Bacteria.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000017148; 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; IPR000121; PEP_util_C.
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.
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|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000732};
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:ERP31703.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017148};
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 8..132
FT /note="Phosphotransferase system enzyme I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05524"
FT DOMAIN 157..229
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 261..541
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 195
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 302
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT BINDING 338
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 588 AA; 66557 MW; 18729C1D233B45E8 CRC64;
MATRKVIQGT AIVRGKGLGK AYFIGRAVQD FTVETIPHHK VVEELDTFEE VRTKVKQYYR
NYNMDTSEGH DESGEGTIMK IYEHIMDDPA FKGQVTEYIS RKNYTVESAV RSVSKEFIDK
FNSAGTSYFR DRSSDMVEIC ETLINFLNNG GNEKYTFSED VVLVIDRSFT PSDIVNYNVN
KIKGVVSKSA GRTSHAAILA RSYSIPVITG VEDIKSRINP HEPVLINAYE DQIIIHPSSD
ECAEYTAYRE RYLQAREVGA KRWHAPAYTP DGVHISVLAN ISFKDDVHMA QDNGADGIGL
VRTEYLLSER ETFPDEEEQF AYYSHIISEQ NSREIVIRVM DIGGDKAAKF LKMPKEGNPF
MGWRAVRILL ERKELFRTQL RAIIRAGQGS NYKIMYPMVT SLSEWREIKQ FTHVVADELG
LPCPPLGILF EVPLAILEID SFLEDIDFAS IGTNDLIQYL SAADRNNSKV NYLYNPAEPA
FLRIVDKAID ACTDKGIPIS ICGEMAGDPM YTIILLGLGL TRFSVIPAMV PIVKEIVSKI
NFLEIQEELS HLLSVTEIDN IADWIEKKNE ELLSDIFERY QIDTVSHD
//
