ID A0A0W7U4B1_9GAMM Unreviewed; 757 AA.
AC A0A0W7U4B1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=ATO46_14225 {ECO:0000313|EMBL:KUE80883.1};
OS Aeromonas schubertii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=652 {ECO:0000313|EMBL:KUE80883.1, ECO:0000313|Proteomes:UP000054876};
RN [1] {ECO:0000313|EMBL:KUE80883.1, ECO:0000313|Proteomes:UP000054876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE80883.1,
RC ECO:0000313|Proteomes:UP000054876};
RA Liu L., Li Q., Zhang F., Shi B.;
RT "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL Submitted (DEC-2015) 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}.
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:KUE80883.1}.
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DR EMBL; LPUO01000006; KUE80883.1; -; Genomic_DNA.
DR RefSeq; WP_050667806.1; NZ_LPUO01000006.1.
DR AlphaFoldDB; A0A0W7U4B1; -.
DR STRING; 652.WL1483_943; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000054876; 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; 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:SF1; PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 1.
DR PANTHER; PTHR46244; 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:KUE80883.1};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUE80883.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..164
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 757 AA; 83877 MW; 6F97AE946050E5A1 CRC64;
MLTQLRHIVE SMTAAASLEQ ALQALVHLTR NVMQVDCCSV YVAEPERRCY RLAATDGLAE
SAVGKAFLPF EEGIVGLVGQ REELINLADA SAHPAFKLLP DVAEEAFRSF LGTPIMHQRQ
VVGILVVQQK ESRLFDEGEE SFLVTLAAQL AARIAHAQAR SQLTRTDWGK PLRGVAGSPG
VAIARAWVWR PRKELAAIVP RKADDPDAQL GRFDQAVEVV RHELEALALR FRESSSQDSV
AIFDIYLHLL ADPSYIKPIR LRIEQEEWTA ISAVKLVSET LIGRFGSMQD PYLRERATDI
KDIALRLISR LVQDEPEHLA ISERVVLVAE EVTATILAEV PRDCLAGVVS IKGSSNSHTA
ILARAMGVPA IMGVEFPLAE IHRLMLVVDG YSGDLFVEPK EPILAEYRQL LHEEQALDQL
VHSTDGQPSE TLDGVKVSLL LNAGLSADTE IAINELADGV GLYRTEIPFM LHDSFPSEWE
QTARYRGILE TYRNRPVCMR TLDVGGDKQL PYFPIVEENP FLGWRGIRLT LDHPELFLVQ
LKAMLRASEG LDNLAVMLPM ISSVGEIRAA RRLLDQAWSE VSQEVATRGG TLHYPPLGVM
IEVPSALYIL PEMAPLIDFW SVGSNDLTQY LLAVDRNNAR VASIYDSFHP AVIRALQLLV
DSARRYGKPV SVCGELAGDP IGVLVLLAMG YRRFSMNTRN IPRIKYVLRN ASLDELVPLL
AEGLRSDSPH ALRGLFSRYL EERGMGGFLR AGHKVTA
//
