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Database: UniProt
Entry: E6WN82_PANSA
LinkDB: E6WN82_PANSA
Original site: E6WN82_PANSA 
ID   E6WN82_PANSA            Unreviewed;       520 AA.
AC   E6WN82;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Phosphoenolpyruvate--protein phosphotransferase {ECO:0000313|EMBL:ADU72867.1};
DE            EC=2.7.3.9 {ECO:0000313|EMBL:ADU72867.1};
GN   OrderedLocusNames=Pat9b_4304 {ECO:0000313|EMBL:ADU72867.1};
OS   Pantoea sp. (strain At-9b).
OG   Plasmid pPAT9B04 {ECO:0000313|EMBL:ADU72867.1,
OG   ECO:0000313|Proteomes:UP000001624}.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU72867.1, ECO:0000313|Proteomes:UP000001624};
RN   [1] {ECO:0000313|EMBL:ADU72867.1, ECO:0000313|Proteomes:UP000001624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-9b {ECO:0000313|EMBL:ADU72867.1,
RC   ECO:0000313|Proteomes:UP000001624};
RC   PLASMID=Plasmid pPAT9B04 {ECO:0000313|Proteomes:UP000001624};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT   "Complete sequence plasmid4 of Pantoea sp. At-9b.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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DR   EMBL; CP002437; ADU72867.1; -; Genomic_DNA.
DR   RefSeq; WP_013512692.1; NC_014841.1.
DR   AlphaFoldDB; E6WN82; -.
DR   KEGG; pao:Pat9b_4304; -.
DR   HOGENOM; CLU_531871_0_0_6; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000001624; Plasmid pPAT9B04.
DR   GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   CDD; cd00367; PTS-HPr_like; 1.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   Gene3D; 3.30.1340.10; HPr-like; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR   InterPro; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_sf.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR008731; PTS_EIN.
DR   InterPro; IPR036618; PtsI_HPr-bd_sf.
DR   PANTHER; PTHR46244:SF4; MULTIPHOSPHORYL TRANSFER PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 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; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
PE   3: Inferred from homology;
KW   Plasmid {ECO:0000313|EMBL:ADU72867.1};
KW   Pyruvate {ECO:0000313|EMBL:ADU72867.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADU72867.1}.
FT   DOMAIN          2..96
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
FT   DOMAIN          375..517
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   520 AA;  57004 MW;  7766270EC667FA61 CRC64;
     MVVELTYQCE ISEGIHARPA GHIARLCNSF QADVVWQNCR TQREANAKSA LSLIATDTLL
     DDKCIITLHG ADALSASQAL ADLLTHLPAF TTVAEPERVS AATSLPRCLR ELQPQYLTGI
     PISGGIAIAP SRFFTGVTFS ELLARSPSAV VKREEEIVRL TAGLHRLRTR KEAALAIAGG
     IEQDLIEAHL LFITDSAFRE SIISYLDTPM NAWSAIVSAA MGFSAILERS SSHYIQERTL
     DMLDIATQLL SEIYGAHARV QPVLSLDAAT IVIADTLTPG QFLALNKQHL AGLILSATGK
     TSHTAILARS QGIPTLADVD VADSHLPSQH EMILDGDQGI LITRTDEKIL RYYRHEIDVQ
     QQMSQKKHQA RTGKPLLTPE VVLWELDVLD KNEVIKKMVD NLWLQQRTDC RDKLCQDIWS
     REVPFPTVVG SGFAIPHARS SAILDSTISV ARLRQPVSWG GVAVDTVFML TISQAAAENE
     HMKYFSTLAR MLMNDEFVAQ AKGAATPEAL YQLIISTLAC
//
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