ID A0A0N0E5V3_9PSED Unreviewed; 839 AA.
AC A0A0N0E5V3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=PF66_00666 {ECO:0000313|EMBL:KPA92925.1};
OS Pseudomonas fuscovaginae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA92925.1, ECO:0000313|Proteomes:UP000037931};
RN [1] {ECO:0000313|EMBL:KPA92925.1, ECO:0000313|Proteomes:UP000037931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA92925.1,
RC ECO:0000313|Proteomes:UP000037931};
RX PubMed=26422147;
RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA Cruz C.V., Oliva R.;
RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL PLoS ONE 10:E0139256-E0139256(2015).
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:KPA92925.1}.
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DR EMBL; JSYZ01000002; KPA92925.1; -; Genomic_DNA.
DR RefSeq; WP_054061880.1; NZ_JSYZ01000002.1.
DR AlphaFoldDB; A0A0N0E5V3; -.
DR STRING; 50340.PF66_00666; -.
DR PATRIC; fig|50340.43.peg.2673; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000037931; 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; IPR023151; PEP_util_CS.
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; PS00742; PEP_ENZYMES_2; 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 Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPA92925.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 26..130
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT DOMAIN 172..259
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 839 AA; 89778 MW; 1D23BD1FAB87E561 CRC64;
MHNNNNELTL GAPLSGPVMP LPAIDDAVFA SGALGEGIAI DPLNDSLHAP CAGVIIHVAR
TRHSLTLRAD NGAELLLHLG LDTVALQGEG FVLLVGEGDR VEAGQALLRF DLDQVARHSR
SLVSPLVLTN GERYELRTRP LDSVKVGDPV LQVVPRQSAQ PSTAMADNGD DEVRGSVRVA
HRGGLHARPA ALLRQTAQGF DCSARLHLGD RSASLDSLIG IMGLGVEEQA QVQVSCRGKD
REAAIQALLQ VLQTPLAEDH HHAVPPQPIA IRPAEAGVLH GVCAAPGLVS GPLARLQAIQ
LPPDCGPHDV EEQRQALTGA LEQVRREIHT TLQQAMARGD HAEQAIFNAH LALLEDPALL
DIAAQAIAHG RAASHAWSQA IESQCQVLLQ LGNPLLAERT NDLRDLRQRV LRILLGDTWH
YELPPGAIVA AHELTPSDLL LISRQDVAGL CMAEGGATSH VAILARAKGL PCLVALGAPL
LEVAPGQQVV LDAGHGRLEL TPDQARLDGV AMAREHHQLR RQRQQELSLS PAHTRDGLSI
EVAANVASAE EAQQAHQSGA DGVGLLRTEF LFVDRQTAPD EREQLNAYQA VVDAMGDKPV
IIRTIDVGGD KQLDYLPLPV EANPVLGLRG IRLAQARPEL LEQQLRALLQ VSPMQRCRIL
LPMVSEVDEL LPIRRCLERL ADELGLSERP QLGVMIEVPC AALLAGQLAE HADFLSIGTN
DLSQYTLAMD RDHAGLAARV DALHPAVLQL IASTCAGAAR HQRWVGVCGA LASDPLATPV
LVGLGVTELS VSPPQIGEIK ERVRSLDAAQ CRRISQSLLQ LGSAASVREA CHQQWPLDR
//
