ID Q49VJ7_STAS1 Unreviewed; 120 AA.
AC Q49VJ7;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN OrderedLocusNames=SSP2068 {ECO:0000313|EMBL:BAE19213.1};
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE19213.1, ECO:0000313|Proteomes:UP000006371};
RN [1] {ECO:0000313|EMBL:BAE19213.1, ECO:0000313|Proteomes:UP000006371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41
RC {ECO:0000313|Proteomes:UP000006371};
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC -!- FUNCTION: Component of the dihydroxyacetone kinase complex, which is
CC responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation
CC of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is
CC phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent
CC reaction, and a phosphorelay system on histidine residues finally leads
CC to phosphoryl transfer to DhaL and dihydroxyacetone.
CC {ECO:0000256|ARBA:ARBA00002788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone
CC phosphate + pyruvate; Xref=Rhea:RHEA:18381, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:16016, ChEBI:CHEBI:57642, ChEBI:CHEBI:58702;
CC EC=2.7.1.121; Evidence={ECO:0000256|ARBA:ARBA00001113};
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DR EMBL; AP008934; BAE19213.1; -; Genomic_DNA.
DR RefSeq; WP_011303715.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49VJ7; -.
DR GeneID; 66868225; -.
DR KEGG; ssp:SSP2068; -.
DR PATRIC; fig|342451.11.peg.2061; -.
DR eggNOG; COG3412; Bacteria.
DR HOGENOM; CLU_045361_2_1_9; -.
DR OrthoDB; 7065393at2; -.
DR Proteomes; UP000006371; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR Gene3D; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR InterPro; IPR039643; DhaM.
DR InterPro; IPR012844; DhaM_N.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR NCBIfam; TIGR02364; dha_pts; 1.
DR PANTHER; PTHR38594; PEP-DEPENDENT DIHYDROXYACETONE KINASE, PHOSPHORYL DONOR SUBUNIT DHAM; 1.
DR PANTHER; PTHR38594:SF1; PEP-DEPENDENT DIHYDROXYACETONE KINASE, PHOSPHORYL DONOR SUBUNIT DHAM; 1.
DR Pfam; PF03610; EIIA-man; 1.
DR SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006371};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..120
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
SQ SEQUENCE 120 AA; 12756 MW; 4D29F8AAB04E2AB1 CRC64;
MTQIVIISHS KAIAAGTKDL LKQMAPGVTV IDQGGVGDDI GTSYDHIQAL INQVDDDTLC
FYDIGSAEMN LDLAIEMYEG QHRVEKVDAP IVEGSFTAAV KLSVGGSIDE TIEALNKTFG
//
