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Database: UniProt
Entry: B7MEF5_ECO45
LinkDB: B7MEF5_ECO45
Original site: B7MEF5_ECO45 
ID   B7MEF5_ECO45            Unreviewed;       321 AA.
AC   B7MEF5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Kinase {ECO:0000313|EMBL:CAR03528.1};
GN   Name=yegV {ECO:0000313|EMBL:CAR03528.1};
GN   OrderedLocusNames=ECS88_2242 {ECO:0000313|EMBL:CAR03528.1};
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR03528.1, ECO:0000313|Proteomes:UP000000747};
RN   [1] {ECO:0000313|Proteomes:UP000000747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000256|RuleBase:RU003704}.
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DR   EMBL; CU928161; CAR03528.1; -; Genomic_DNA.
DR   RefSeq; WP_000011933.1; NC_011742.1.
DR   AlphaFoldDB; B7MEF5; -.
DR   KEGG; ecz:ECS88_2242; -.
DR   HOGENOM; CLU_027634_7_1_6; -.
DR   OMA; IGGCALN; -.
DR   Proteomes; UP000000747; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01944; YegV_kinase_like; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR10584:SF166; RIBOKINASE; 1.
DR   PANTHER; PTHR10584; SUGAR KINASE; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS00583; PFKB_KINASES_1; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003704};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000747};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003704}.
FT   DOMAIN          19..306
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   321 AA;  34385 MW;  7643AEAAFEABA66A CRC64;
     MSGARLHTLL PELATHQPVM VVGAAVIDVI ADAYALPWRG CDIELKQQSV NVGGCALNIA
     VALKRLGIEA GNALPLGQGV WAEIIRNRMA KEDLISLIDN AEGDNGWCLA LVEPDGERTF
     MSFSGVENQW NRQWLARLTV APGSLLYFSG YQLASPCGEL LVEWLEKLQD VTPFIDFGPR
     IGDIPDALLA RIMACRPLVS LNRQEAEIAA ERFALSAEIT TLGKQWQEKF AAPLIVRLDK
     EGAWYFSNDA SGCIPAFPTQ VVDTIGAGDS HAGGVLAGLA SGLPLADAVL LGNAVASWVV
     GHRGGDCAPT REELLLAHKN V
//
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