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Database: UniProt
Entry: E2X7J9_SHIDY
LinkDB: E2X7J9_SHIDY
Original site: E2X7J9_SHIDY 
ID   E2X7J9_SHIDY            Unreviewed;       748 AA.
AC   E2X7J9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=Asd1617_04079 {ECO:0000313|EMBL:AHA66906.1};
OS   Shigella dysenteriae 1617.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=754093 {ECO:0000313|EMBL:AHA66906.1, ECO:0000313|Proteomes:UP000031647};
RN   [1] {ECO:0000313|EMBL:AHA66906.1, ECO:0000313|Proteomes:UP000031647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1617 {ECO:0000313|EMBL:AHA66906.1,
RC   ECO:0000313|Proteomes:UP000031647};
RA   Aksomboon Vongsawan A., Kapatral V., Vaisvil B., Serichantalergs O.,
RA   Hale T.L., Mason C.J.;
RT   "Comparative genomics of Sd1617 to representative strains in evaluating its
RT   pathogenesis.";
RL   Submitted (SEP-2013) 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; CP006736; AHA66906.1; -; Genomic_DNA.
DR   RefSeq; WP_000957899.1; NZ_ADUT01000021.1.
DR   AlphaFoldDB; E2X7J9; -.
DR   KEGG; sdz:Asd1617_04079; -.
DR   PATRIC; fig|754093.4.peg.3970; -.
DR   HOGENOM; CLU_007308_7_1_6; -.
DR   Proteomes; UP000031647; Chromosome.
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; IPR018274; PEP_util_AS.
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; 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.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 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:AHA66906.1};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHA66906.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
SQ   SEQUENCE   748 AA;  83795 MW;  CF95B550AE8022CF CRC64;
     MLTRLREIVE KVASAPRLNE ALNILVTDIC LAMDTEVCSV YLADHDRRCY YLMATRGLKK
     PRGRTVTLAF DEGIVGLVGR LAEPINLADA QKHPSFKYIP SVKEERFRAF LGVPIIQRRQ
     LLGVLVVQQR ELRQYDESEE SFLVTLATQM AAILSQSQLT ALFGQYRQTR IRALPAAPGV
     AIAEGWQDAT LPLMEQEYQA STLDPALERE RLTGALEEAA NEFRRYSKRF AAGAQKETAA
     IFDLYSHLLS DTRLRRELFA EVDKGSVAEW AVKTVIEKFA EQFAVLSDNY LKERAVDLRA
     LGQRLLFHLD DANQGPNAWP ERFILVADEL SATTLAELPQ DRLVGVVVRD GAANSHAAIM
     VRALGIPTVM GADIQPSVLH CRTLIVDGYR GELLVDPEPV LLQEYQRLIS EEIELSRLAE
     DDVNLPAQLK SGERIKVMLN AGLSPEHEEK LGSRIDGIGL YRTEIPFMLQ SGFPSEEEQV
     AQYQGMLQMF NDKPVTLRTL DVGADKQLPY MPISEENPCL GWRGIRITLD QPEIFLIQVR
     AMLRANAATG NLNILLPMVT SLDEVDEARR LIERAGREVE EMIGYEIPKP RIGIMLEVPS
     MVFMLEHLAK RVDFISVGTN DLTQYILAVD RNNTRVANIY DSLHPAMLRA LAMIAREAEI
     HGIDLRMCGE MAGDPMCVAI LIGLGYRHLS TNGRSVARVK YLLRRIDFAE AENLAQRSLE
     AQLATEVRHQ VAAFMERRGM GGLIRGGL
//
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