ID   A0A212QZY3_9PROT        Unreviewed;       787 AA.
AC   A0A212QZY3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=SAMN07250955_104235 {ECO:0000313|EMBL:SNB65302.1};
OS   Arboricoccus pini.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Arboricoccus.
OX   NCBI_TaxID=1963835 {ECO:0000313|EMBL:SNB65302.1, ECO:0000313|Proteomes:UP000197065};
RN   [1] {ECO:0000313|EMBL:SNB65302.1, ECO:0000313|Proteomes:UP000197065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B29T1 {ECO:0000313|EMBL:SNB65302.1,
RC   ECO:0000313|Proteomes:UP000197065};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FYEH01000004; SNB65302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212QZY3; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000197065; Unassembled WGS sequence.
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; IPR023151; PEP_util_CS.
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.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000197065};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SNB65302.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          42..188
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   787 AA;  86483 MW;  3BA12824BFDC63E0 CRC64;
     MTGPYVNRTT SDQGAEPRRG AEFGSARRLL RRLIEVVAEQ ISPQQRLDRI VKMIAANLVA
     EVCSVYAQRA GDVIELFATE GLAGEAVHHV RMRVGEGLVG RIAATGVVIN TADAQGHPNF
     RYFPETREEN YASFLGVPIL RSGRVVGVLT VQNSARRIYS EEEVEALQII ASVLAEMFAS
     GGLVDPAQYG DVPGLSHEPQ RLEGRRLVDG VAVGHAFLHE ARVEIERLLS DDPAYERDRV
     DAAMEELKAS LDAMLARSDL AAGEHREVLE TYRMVAQDTG WRRRIREAVD TGLSAEAAVR
     RVQEETRLRI GHASDPYLRE RLLDLDDLAN RLLRHLTGAA LQGPADLPDD AIIVARNLSA
     AELVEYDRTR LRGIILEEGS LTAHVTIVAR AFNIPVVGRV DSAMSLIESG DIVALDGSHG
     TLFLRPTDDV LHAFTRTVQL QAEQRQAYQA LRVQPAITLD GIKIRLSINA AFLADLVGFE
     ESGADGIGLF RTELAFMTRS TLPTVADQAA HYRDVLDRTQ GKPVIFRTLD IGSDKQVSYW
     RMPAEDNPAL GWRAMRMMLD RPAILAAQLR AMARAAAERE LYIMFPMVAD VDELIAARRI
     LDREVNQARL AGQGPRQVTV GVMLEVPALM FQLDDLLPLI DFVSVGTNDL AQFLFACDRG
     NPAVAERYDL LSPALLNLIE HLAQRCQAYG VSLGVCGEMA SRPIEAMALV ALGVHHLSVV
     ASEIGPIKAM IRSLDASRLR EFLHTARNWA GRRTGGSHLR ASMIDWAVDH GIALPDIGTW
     ATTLDPQ
//