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Database: UniProt
Entry: Q31XF8_SHIBS
LinkDB: Q31XF8_SHIBS
Original site: Q31XF8_SHIBS 
ID   Q31XF8_SHIBS            Unreviewed;       748 AA.
AC   Q31XF8;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
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:ABB67250.1};
GN   OrderedLocusNames=SBO_2721 {ECO:0000313|EMBL:ABB67250.1};
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268 {ECO:0000313|EMBL:ABB67250.1, ECO:0000313|Proteomes:UP000007067};
RN   [1] {ECO:0000313|EMBL:ABB67250.1, ECO:0000313|Proteomes:UP000007067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227 {ECO:0000313|EMBL:ABB67250.1,
RC   ECO:0000313|Proteomes:UP000007067};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000036; ABB67250.1; -; Genomic_DNA.
DR   RefSeq; WP_000957921.1; NC_007613.1.
DR   AlphaFoldDB; Q31XF8; -.
DR   KEGG; sbo:SBO_2721; -.
DR   HOGENOM; CLU_007308_7_1_6; -.
DR   Proteomes; UP000007067; 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   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          17..164
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   748 AA;  83742 MW;  2FCEC72F348B014C CRC64;
     MLTRLREIVE KVASAPRLNE ALNILVTDIC LAMDTEVCSV YLADHDRRCY YLMATRGLKK
     PRGRTVTLAF DEGIVGLVGR LAEPINLADA QKHPSFKYIP SVKEERFRAF LGVPIIQRRQ
     LLGVLVVQQR ELRQYDESEE SFLVTLATQM AAILSQSQLT ALFGQYRQTR IRALPAAPGV
     AIAEGWQDAT LPLMEQVYQA STLDPALERE RLTGALEEAA NEFRRYSKRF AAGAQKETAA
     IFDLYSHLLS DTRLRRELFA EVDKGSVAEW AVKTVIEKFA EQFAALSDNY LKERAGDLRA
     LGQRLLFHLD DANQGPNAWP ERFILVADEL SATTLAELPQ DRLVGVVVRD GAANSHAAIM
     VRALGLPTVM GADIQPSVLH RRTLIVDGYR GELLVDPEPI LLQEYQRLIS EEIELSRLAE
     DDVNLPAQLK SGERIKVMLN AGLSPEHEEK LGSRIDGIGL YRTEIPFMLQ SGFPSEEEQV
     AQYQGMLQMF NDKPVTLRTL DVGADKQLPY MPISEENPCL GWRGIRITLD QPEIFLIQVR
     AMLRANAATG NLNILLPMVT SLDEVDEARR LIERAGREVE EMIGYEIPKP RIGIMLEVPS
     MVFMLPHLAK RVDFISVGTN DLTQYILAVD RNNTRVANIY DSLHPAMLRA LAMIAREAEI
     HGIDLRLCGE MAGDPMCVAI LIGLGYRHLS MNGRSVARVK YLLRRIDFAE AENLAQRSLE
     AQLATEVRHQ VAAFMERRGM GGLIRGGL
//
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