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Database: UniProt
Entry: A0A0A7FVW1_9CLOT
LinkDB: A0A0A7FVW1_9CLOT
Original site: A0A0A7FVW1_9CLOT 
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
//
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