ID A0A3N3ZQ42_9MICC Unreviewed; 888 AA.
AC A0A3N3ZQ42;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:ROZ62300.1};
GN ORFNames=EDL96_10280 {ECO:0000313|EMBL:ROZ62300.1};
OS Kocuria soli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=2485125 {ECO:0000313|EMBL:ROZ62300.1, ECO:0000313|Proteomes:UP000270616};
RN [1] {ECO:0000313|EMBL:ROZ62300.1, ECO:0000313|Proteomes:UP000270616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M5W7-7 {ECO:0000313|EMBL:ROZ62300.1,
RC ECO:0000313|Proteomes:UP000270616};
RA Tuo L.;
RT "Kocuria sp. M5W7-7, whole genome shotgun sequence.";
RL Submitted (OCT-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}.
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:ROZ62300.1}.
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DR EMBL; RKMF01000013; ROZ62300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N3ZQ42; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000270616; 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 CDD; cd00367; PTS-HPr_like; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR Gene3D; 3.30.1340.10; HPr-like; 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; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_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; IPR001127; PTS_EIIA_1_perm.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR002114; PTS_HPr_Ser_P_site.
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; TIGR00830; PTBA; 1.
DR NCBIfam; TIGR01003; PTS_HPr_family; 1.
DR NCBIfam; TIGR01417; PTS_I_fam; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF00381; PTS-HPr; 1.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55594; HPr-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 1.
DR PROSITE; PS00589; PTS_HPR_SER; 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:ROZ62300.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000270616};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ROZ62300.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 28..132
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT DOMAIN 199..286
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
FT REGION 302..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 92165 MW; AF56650DF40ACAAB CRC64;
MSDPTTATRI DFIAPLTGVL VPIEEVPDPV FAQKMMGEGF SIDPLAGQLV APVAGEVVDV
QQSGHAVTVR SEDGLDVLMH IGLDTVALQG QGFTPLVEQG QRVTVGQPLI DFELDFLATR
AKSLLTQIVI ANSDRVDSLS PKSGLVKAGQ DVAAEVVLAG ESTNDGAAGS TAAGVAAGAG
AGVAAGAAAG AASAGGSDTA IAEVIIPNPT GMHARPAANL VNVAKDFESD IQLDKEDESG
SAKSIVSILA MALAFGDKMT ITATGPDAQQ AVTALTEAIN GGLGEDVGTL PSGTADTLAT
PAVEEPSQAE PVHVTDEPRS GDPNVLLGVT ASPGLGIGRV VQMRQTEIQV QETGEDPGQE
RAKLDAAIQT SINELGALQQ RLVNEGSEDK AEIFGAHQEI LRDPELVNQA QTGIDQGKSA
AFAWRESYTG FATQLEGLQN EVLAGRAADM RDVGQRVLET LTGQHREQAE LAEGTILVAE
DLTPSDTAQL DRSKVVGFAT TQGGASSHVA IIARSMDIPA VAGIEARALD IAEGSRVVLD
GTAGKLQVNL SDEEIAGIEA RQQRMAERKA VEDAAKDEPA VTTDGHQVAV VANIGGADDA
REAMQHGAEG VGLLRSEFVF MERPTAPTEQ EQADVYAECS RALKPGQPLV LRTLDVGGDK
PLSYLPIPKE ENPFLGLRGV RVGLEQPEVL RTQLRAIFAA AGAGAELHVM FPMIATIADW
RAAKAIFDEE KAASGITTKV SCGIMMEVPS VAVMAQQFAA EEGCDFFSVG TNDLTSYTLA
MDRGHPKLAA QVDPCNPAVL TLIGQAAAAL HAQGKWLGVC GGVASDPQAV PILVGLGVDE
LSASIPAIPS VKAKVREYSL EQCKELAAQA VTCSTPEEVR SLVPMDQD
//
