ID   PTSA_BACSU              Reviewed;         168 AA.
AC   P50829;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 139.
DE   RecName: Full=Phosphotransferase enzyme IIA component PtsA {ECO:0000305};
DE   AltName: Full=PTS system EIIA component {ECO:0000305};
GN   Name=ptsA {ECO:0000303|PubMed:30038046}; Synonyms=ypqE;
GN   OrderedLocusNames=BSU22230;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA   Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA   Serror P.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   serA and kdg loci cloned in a yeast artificial chromosome.";
RL   Microbiology 142:2005-2016(1996).
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   FUNCTION, AND DOMAIN.
RX   PubMed=30038046; DOI=10.1128/jb.00213-18;
RA   Morabbi Heravi K., Altenbuchner J.;
RT   "Cross talk among transporters of the phosphoenolpyruvate-dependent
RT   phosphotransferase system in Bacillus subtilis.";
RL   J. Bacteriol. 200:0-0(2018).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane
CC       (Probable). Plays an important role in the phosphorylation of EIIA-
CC       deficient PTS transporters (PubMed:30038046). The EIIA domain can
CC       transfer a phosphoryl group to EIIA-deficient PTS transporters,
CC       enabling growth with maltose, N-acetylglucosamine, sucrose or trehalose
CC       as the sole carbon source (PubMed:30038046).
CC       {ECO:0000269|PubMed:30038046, ECO:0000305|PubMed:30038046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The PTS EIIA type-1 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue (PubMed:30038046). Then, it transfers the phosphoryl
CC       group to the PTS EIIB type-1 domain (PubMed:30038046).
CC       {ECO:0000269|PubMed:30038046}.
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DR   EMBL; L47838; AAB38467.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14140.1; -; Genomic_DNA.
DR   PIR; H69940; H69940.
DR   RefSeq; NP_390105.1; NC_000964.3.
DR   RefSeq; WP_009967573.1; NC_000964.3.
DR   AlphaFoldDB; P50829; -.
DR   SMR; P50829; -.
DR   FunCoup; P50829; 142.
DR   STRING; 224308.BSU22230; -.
DR   TCDB; 4.A.1.1.21; the pts glucose-glucoside (glc) family.
DR   PaxDb; 224308-BSU22230; -.
DR   EnsemblBacteria; CAB14140; CAB14140; BSU_22230.
DR   GeneID; 939046; -.
DR   KEGG; bsu:BSU22230; -.
DR   PATRIC; fig|224308.179.peg.2427; -.
DR   eggNOG; COG2190; Bacteria.
DR   InParanoid; P50829; -.
DR   OrthoDB; 92465at2; -.
DR   PhylomeDB; P50829; -.
DR   BioCyc; BSUB:BSU22230-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P50829; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR   FunFam; 2.70.70.10:FF:000001; PTS system glucose-specific IIA component; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR001127; PTS_EIIA_1_perm.
DR   InterPro; IPR050890; PTS_EIIA_component.
DR   NCBIfam; TIGR00830; PTBA; 1.
DR   PANTHER; PTHR45008; PTS SYSTEM GLUCOSE-SPECIFIC EIIA COMPONENT; 1.
DR   PANTHER; PTHR45008:SF1; PTS SYSTEM GLUCOSE-SPECIFIC EIIA COMPONENT; 1.
DR   Pfam; PF00358; PTS_EIIA_1; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR   PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
PE   4: Predicted;
KW   Cytoplasm; Kinase; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..168
FT                   /note="Phosphotransferase enzyme IIA component PtsA"
FT                   /id="PRO_0000186711"
FT   DOMAIN          36..140
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        88
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
SQ   SEQUENCE   168 AA;  17936 MW;  7E3AC146345B0D17 CRC64;
     MLKKLFGMGK IQEKVTEEVI YSPADGTVMD LSDVPDPVFS QKMMGEGIAV EPSSGEIVSP
     AEGEVIQIFH TKHAVGIRTR SGIELLIHVG LETVNMNGEG FTAHIKEGDK VKVGDPLITC
     DLELIKEKAS STVIPIVIMN GEAVGSMVSA GEKAARKGES KLFTIKAK
//