ID A0A345RDL8_9RHOB Unreviewed; 747 AA.
AC A0A345RDL8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN Name=ptsP {ECO:0000313|EMBL:AXI55655.1};
GN ORFNames=C1J05_15100 {ECO:0000313|EMBL:AXI55655.1};
OS Sulfitobacter sp. JL08.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=2070369 {ECO:0000313|EMBL:AXI55655.1, ECO:0000313|Proteomes:UP000253748};
RN [1] {ECO:0000313|EMBL:AXI55655.1, ECO:0000313|Proteomes:UP000253748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL08 {ECO:0000313|EMBL:AXI55655.1,
RC ECO:0000313|Proteomes:UP000253748};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter genomes from the North Sea.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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; CP025815; AXI55655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345RDL8; -.
DR KEGG; suli:C1J05_15100; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000253748; Chromosome.
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 Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
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; PF01590; GAF; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55781; GAF domain-like; 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Pyruvate {ECO:0000313|EMBL:AXI55655.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253748};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AXI55655.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..171
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 747 AA; 82217 MW; CC85B572816031A4 CRC64;
MPERTESESR RLLGRLRDAM ASDEAGQARL NKITHLIADS MRSEVCSIYL FRDDVTLELC
ATEGLKPESV HQTRMKLGEG LVGRVAKSRQ IINTPNAPGA KGFRYMPETG EEVFSSFLGI
PVQRLGEALG VLVVQSREAR EFSADEVYAL EVVAMVLAEM TELGAFVGEG AALSARHQQP
VLIRGTTGQE GAAEGHVWLH EPRVVVANPI ADDPAVELKR LQNAVEELRV GVDKMLDMAA
IGDKEQRQVL EAYRMFANSK GWMRRMEEDI ARGLSAEAAV EKEQSLARSR IGQAQDSYLR
ERLSDLDDLS NRLLRILTGQ GSETGAEMPA DPILIARNIG PAELLDYGRS LRGIVLEEGS
VGSHAAIVAR ALAIPLVVRA GRIISEALNG DHVMVDGDQG VVHLRPDDSV VTAFRDKIAM
QADALERYAS IRDKPAETRC GAVIGMHMNA GLMADLPSLD GSGAEGVGLF RTELQFLVRN
KMPTRTELAA LYARVLDAAH GKRVVFRTLD IGSDKVLPYM KPTDEPNPAL GWRAIRVGLD
KPGIMRMQLQ ALLRAANGRP LTVMFPFVAQ FEEYRAARAE VDKTIAREKR LGHVLPETIE
IGAMLETPSL AFAPQKFFDE VEFLSIGGND LKQFFFAADR ENERVRRRYD TLNVSFLSLI
EKIVERCAIS NTPLSFCGED AGRPIEAMCL AAIGLRTLSM RPASIGPVKS LLRRVNLDEV
RQVIADARHR GDMSVRPAIM EYLRAQG
//