ID A0A0A7FVW1_9CLOT Unreviewed; 148 AA.
AC A0A0A7FVW1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ascorbate-specific PTS system EIIA component {ECO:0000256|ARBA:ARBA00041175};
DE AltName: Full=Ascorbate-specific phosphotransferase enzyme IIA component {ECO:0000256|ARBA:ARBA00042072};
GN ORFNames=U729_509 {ECO:0000313|EMBL:AIY83713.1};
OS Clostridium baratii str. Sullivan.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY83713.1, ECO:0000313|Proteomes:UP000030635};
RN [1] {ECO:0000313|EMBL:AIY83713.1, ECO:0000313|Proteomes:UP000030635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY83713.1};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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. The
CC enzyme II UlaABC PTS system is involved in ascorbate transport.
CC {ECO:0000256|ARBA:ARBA00037387}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP006905; AIY83713.1; -; Genomic_DNA.
DR RefSeq; WP_039311350.1; NZ_CP006905.1.
DR AlphaFoldDB; A0A0A7FVW1; -.
DR STRING; 1561.NPD11_2480; -.
DR KEGG; cbv:U729_509; -.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_072531_2_0_9; -.
DR OrthoDB; 369398at2; -.
DR Proteomes; UP000030635; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR PANTHER; PTHR36203; ASCORBATE-SPECIFIC PTS SYSTEM EIIA COMPONENT; 1.
DR PANTHER; PTHR36203:SF1; ASCORBATE-SPECIFIC PTS SYSTEM EIIA COMPONENT; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Pyruvate {ECO:0000313|EMBL:AIY83713.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030635};
KW Transferase {ECO:0000313|EMBL:AIY83713.1}.
FT DOMAIN 4..147
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
SQ SEQUENCE 148 AA; 16503 MW; 570F78810DADC481 CRC64;
MLGELVTKDV IKVNEKCDNW KDAIGVGVEL LESKGIVEDR YKDAIINNFK ELGPYMVIAP
GIVLSHARPE GGVNETGISI LTLEEPLNFG NEQNDPVKLV VTLAAKDNEN HLELLSSLME
MFMNTEDLNG ILEADNQNEV YKIIQKYN
//