ID A0A1D9M9Y4_9RHOB Unreviewed; 746 AA.
AC A0A1D9M9Y4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=LPB142_04385 {ECO:0000313|EMBL:AOZ68647.1};
OS Rhodobacter sp. LPB0142.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1850250 {ECO:0000313|EMBL:AOZ68647.1, ECO:0000313|Proteomes:UP000176562};
RN [1] {ECO:0000313|EMBL:AOZ68647.1, ECO:0000313|Proteomes:UP000176562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0142 {ECO:0000313|EMBL:AOZ68647.1,
RC ECO:0000313|Proteomes:UP000176562};
RA Kim E., Yi H.;
RT "Rhodobacter sp. LPB0142, isolated from sea water.";
RL Submitted (OCT-2016) 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; CP017781; AOZ68647.1; -; Genomic_DNA.
DR RefSeq; WP_071165628.1; NZ_CP017781.1.
DR AlphaFoldDB; A0A1D9M9Y4; -.
DR STRING; 1850250.LPB142_04385; -.
DR KEGG; rhp:LPB142_04385; -.
DR Proteomes; UP000176562; 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; PF13185; GAF_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:AOZ68647.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000176562};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AOZ68647.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..171
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT COILED 218..245
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 746 AA; 81972 MW; 41C693C1239B103B CRC64;
MGLRRDSDSR SLLRRLRDTL ATPGGGQDRL DKITHLIADS MGTQVCSIYL FRDRETLELC
ATEGLNPESV HQTRMRLGEG LVGRVARAGA PVNTGNAPAE PGFRYMPETG EEIYSSFLGV
PIQRVGEKLG VLVVQSREAR EFSDDEVYGL EVVAMVLAEM TELGAFTGEG NGIGATHRFP
VLFRGATGQE GAAEGHVWLH EPRVVVTNPV GDDPETETRR LEEAVVQLQA QIDEMLETAA
TADKEQRQVL ETYKMFAHSR GWLRRMQEDI GLGLSAEAAV EKEQSTARAR LEQSPDPYLR
ERLNDLDDLS NRLLRLLTGQ GKDTGAELPP DPVLVARNIG PAELLEYGRA LKGVVLEEGS
VGSHAAIVAR ALSIPLVIHA SRITAEALNG DPILVDGDQG IVHLRPEDTV AAAFRDKIAM
QAEAQKRYAD LRELPAEDRS GRVIRLMMNA GLMADLPSLT GSGADGVGLF RTELQFLIRS
RVPRRAELAA LYKRVMDAAG EKRVQFRTLD IGSDKVLPYM KPQDEPNPAM GWRAIRVGLD
KPGVLRMQLQ ALVRAAEGRP LSVMFPFIAT PEEFYTARES LLHEVEREAS MGRPVPADLK
IGAMLETPSL AFAPDSFFET CDFISIGGND LKQFFFAADR ENERVRRRYD TLDTSFLTFI
EKIVARCAAH DTQLSFCGED AGRPVEALTF AALGLKTLSM RPASIGPVKH LIRRANLAEL
REVILAERSA GAQSVRPAVM HYLAGL
//