ID A0A0P1INB2_9RHOB Unreviewed; 753 AA.
AC A0A0P1INB2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN Name=ptsI {ECO:0000313|EMBL:CUK25061.1};
GN ORFNames=TA5114_00851 {ECO:0000313|EMBL:CUK25061.1};
OS Cognatishimia activa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatishimia.
OX NCBI_TaxID=1715691 {ECO:0000313|EMBL:CUK25061.1, ECO:0000313|Proteomes:UP000051184};
RN [1] {ECO:0000313|Proteomes:UP000051184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5114 {ECO:0000313|Proteomes:UP000051184};
RA Rodrigo-Torres Lidia, Arahal R.David.;
RL Submitted (SEP-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}.
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DR EMBL; CYUE01000006; CUK25061.1; -; Genomic_DNA.
DR RefSeq; WP_058314062.1; NZ_CYUE01000006.1.
DR AlphaFoldDB; A0A0P1INB2; -.
DR STRING; 1715691.TA5113_02501; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000051184; 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; 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 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:CUK25061.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051184};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUK25061.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 29..175
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 753 AA; 82971 MW; EC167F69E6110344 CRC64;
MAQNLNKNFE SESRKLLLRL REAMAEDSAG QARLDKITGL IASSMGTEVC SIYLFRDEET
LELCATEGLN PDSVHQTRLR IGEGLVGRVA RHSRVVNTAD APSERGFRYM PETGEEIYSS
FCGIPIQRLG ENMGVLVVQS REARDFSSDE VYALEVVAMV LAEMTELGAF VGEGAALSPL
HQQSVLIRGG TGQEGVAVGH VWLHEPRVVV SNPIADDPEA EQKRLEDAIE ELRVGVDRML
EGAAGGDKEQ LQVLEAYRMF ANSKGWMKRM EQDISQGLSA EAAVEKEQSI ARSRMAKATD
AYLRDRLHDL DDLSNRLLRI LTGQGKDTGA EMPENPILVA RNIGPAELLE YDRKLKGVVL
EEGSVGSHAA IVARALAIPL IVHADRITTE ALNGDAIMVD GDEGVVHLRP DESVATAFRD
KMAMRTNAQK RYASIREKPA ETLDGTTIHL QMNAGLMADL PSLEGSGAEG VGLFRTELQF
LIRNQMPKRT ELAEIYSKVM DSAKGKRVVF RTLDIGSDKV LPYMAPQDEP NPALGWRAIR
VGLDKPGVLR MQLQALLRAA NGRPLTVMFP FIAQFEEFRA AKAEMEKAVE RERRLGHILP
DTLDVGAMLE TPSLGFAPQK FFEEVGFISI GGNDLKQFFF AADRENERVR RRYDTLNVSF
LTFIEGIVNR CNSTKTPVSF CGEDAGRPLE AVCLAAMGLR NLSMRPASIG PVKSILRRTN
LAEVRKIIVD ARERGDQSVR AAVKAYLKET GAL
//