ID   PPS_BACSU               Reviewed;         866 AA.
AC   O34309; O69265; Q796E8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Putative phosphoenolpyruvate synthase;
DE            Short=Putative PEP synthase;
DE   AltName: Full=Pyruvate, water dikinase;
GN   Name=pps; OrderedLocusNames=BSU18830;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich D.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   terC and odhAB loci cloned in a yeast artificial chromosome.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-854.
RC   STRAIN=168;
RX   PubMed=7704256; DOI=10.1099/13500872-141-2-281;
RA   Wolf M., Geczi A., Simon O., Borriss R.;
RT   "Genes encoding xylan and beta-glucan hydrolysing enzymes in Bacillus
RT   subtilis: characterization, mapping and construction of strains deficient
RT   in lichenase, cellulase and xylanase.";
RL   Microbiology 141:281-290(1995).
CC   -!- FUNCTION: Might catalyze the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC   -!- CAUTION: Lacks almost all of the known catalytic and substrate-binding
CC       residues for this enzyme; hence it is annotated as putative.
CC       {ECO:0000305}.
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DR   EMBL; AF027868; AAB84457.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13775.1; -; Genomic_DNA.
DR   EMBL; Z34519; CAA84277.1; -; Genomic_DNA.
DR   PIR; F69681; F69681.
DR   RefSeq; NP_389764.1; NC_000964.3.
DR   RefSeq; WP_003231379.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34309; -.
DR   SMR; O34309; -.
DR   STRING; 224308.BSU18830; -.
DR   PaxDb; O34309; -.
DR   EnsemblBacteria; CAB13775; CAB13775; BSU_18830.
DR   GeneID; 939985; -.
DR   KEGG; bsu:BSU18830; -.
DR   PATRIC; fig|224308.179.peg.2053; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG3848; Bacteria.
DR   InParanoid; O34309; -.
DR   OMA; WTRKIAA; -.
DR   PhylomeDB; O34309; -.
DR   BioCyc; BSUB:BSU18830-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..866
FT                   /note="Putative phosphoenolpyruvate synthase"
FT                   /id="PRO_0000378089"
FT   REGION          410..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        825
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        267..272
FT                   /note="AQTLTD -> GSNTELI (in Ref. 3; CAA84277)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        625..645
FT                   /note="RQEALKKEQELLDRLKQLPDG -> ATGSFEERTRVIRSIEAITGC (in
FT                   Ref. 3; CAA84277)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        850
FT                   /note="D -> H (in Ref. 3; CAA84277)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   866 AA;  97192 MW;  5C1D3BC30F074DEA CRC64;
     MSSLVLGLHE IEKTQLSLVG GKGLHLGELS KIQGIQVPEG FCVTTVGYQK AIEQNETLQV
     LLDQLTMLKV EDRDQIGNIS RKIRQIIMEV DIPSDVVKAV AQYLSQFGEE HAYAVRSSAT
     AEDLPHASFA GQQDTYLNIT GVDAILQHIS KCWASLFTDR AVIYRMQNGF DHSQVYLSVI
     VQRMVFPQAS GILFTADPIT SNRKVLSIDA GFGLGEALVS GLVSADCFKV QDGQIIDKRI
     ATKKMAIYGR KEGGTETQQI DSDQQKAQTL TDEQILQLAR IGRQIEAHFG QPQDIEWCLA
     RDTFYIVQSR PITTLFPIPE ASDQENHVYI SVGHQQMMTD PIKPLGLSFF LLTTVAPMRK
     AGGRLFVDVT HHLASPDSRE VFLKGMGQHD QLLKDALMTI IKRRDFIKSI PNDKTAPNPS
     RGNADMPAQV ENDPTIVSDL IESSQTSIEE LKQNIQTKSG SDLFRFILED IQELKKILFN
     PKSSVLIRTA MNASLWINEK MNEWLGEKNA ADTLSQSVPH NITSEMGLAL LDVADVIRPY
     PEVIDYLQHV KDDNFLDELA KFDGGSKTRD AIYDYLSKYG MRCTGEIDIT RTRWSEKPTT
     LVPMILNNIK NFEPNVGHRK FEQGRQEALK KEQELLDRLK QLPDGEQKAK ETKRAIDIIR
     NFSGFREYPK YGMVNRYFVY KQALLKEAEQ LIEAGVIHEK EDIYYLTFEE LHEVVRTHKL
     DYQIISTRKD EYTLYEKLSP PRVITSDGEI VTGEYKRENL PAGAIVGLPV SSGVIEGRAR
     VILNMEDADL EDGDILVTSF TDPSWTPLFV SIKGLVTEVG GLMTHGAVIA REYGLPAVVG
     VENAAKLIKD GQRIRVHGTE GYIEIF