ID   PTFAH_VIBCH             Reviewed;         400 AA.
AC   Q9KM70;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Multiphosphoryl transfer protein {ECO:0000250|UniProtKB:P44715};
DE            Short=MTP {ECO:0000250|UniProtKB:P44715};
DE   Includes:
DE     RecName: Full=PTS system fructose-specific EIIA component {ECO:0000250|UniProtKB:P69811};
DE     AltName: Full=EIIA-Fru {ECO:0000250|UniProtKB:P17127};
DE     AltName: Full=EIII-Fru {ECO:0000250|UniProtKB:P17127};
DE     AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69811};
DE   Includes:
DE     RecName: Full=Phosphocarrier protein HPr {ECO:0000250|UniProtKB:P17127};
DE              Short=Protein H {ECO:0000250|UniProtKB:P17127};
GN   Name=fruB {ECO:0000303|PubMed:33476373};
GN   OrderedLocusNames=VC_A0518 {ECO:0000312|EMBL:AAF96421.1};
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=33476373; DOI=10.1093/nar/gkab013;
RA   Yoon C.K., Kang D., Kim M.K., Seok Y.J.;
RT   "Vibrio cholerae FruR facilitates binding of RNA polymerase to the fru
RT   promoter in the presence of fructose 1-phosphate.";
RL   Nucleic Acids Res. 49:1397-1410(2021).
RN   [3]
RP   INDUCTION.
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=33649152; DOI=10.1128/jb.00044-21;
RA   Beck C., Perry S., Stoebel D.M., Liu J.M.;
RT   "Cra and cAMP receptor protein have opposing roles in the regulation of
RT   fruB in Vibrio cholerae.";
RL   J. Bacteriol. 203:0-0(2021).
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 FruAB PTS system is involved in fructose transport.
CC       {ECO:0000250|UniProtKB:P69811}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P69811}.
CC   -!- INDUCTION: Part of the fruBKA (fru) operon, which is induced in the
CC       presence of fructose via the FruR (Cra) regulatory protein
CC       (PubMed:33476373). Transcription is repressed by FruR in the absence of
CC       fructose (PubMed:33649152). CRP activates expression of the fru operon
CC       in the absence of glucose (PubMed:33649152). The two regulators can
CC       work independently to control the expression of the operon depending on
CC       carbon source availability (PubMed:33649152).
CC       {ECO:0000269|PubMed:33476373, ECO:0000269|PubMed:33649152}.
CC   -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC   -!- DOMAIN: In contrast to classical PTS systems, the fructose-specific PTS
CC       has no requirement for HPr; FruB combines a IIA domain with a HPr
CC       domain. {ECO:0000250|UniProtKB:P69811}.
CC   -!- DISRUPTION PHENOTYPE: Does not affect growth on glucose. Mutant shows a
CC       slight growth retardation on fructose. {ECO:0000269|PubMed:33476373}.
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DR   EMBL; AE003853; AAF96421.1; -; Genomic_DNA.
DR   PIR; D82450; D82450.
DR   RefSeq; NP_232909.1; NC_002506.1.
DR   RefSeq; WP_000891934.1; NZ_LT906615.1.
DR   SMR; Q9KM70; -.
DR   STRING; 243277.VC_A0518; -.
DR   DNASU; 2612791; -.
DR   EnsemblBacteria; AAF96421; AAF96421; VC_A0518.
DR   GeneID; 57741922; -.
DR   KEGG; vch:VC_A0518; -.
DR   PATRIC; fig|243277.26.peg.3144; -.
DR   eggNOG; COG1925; Bacteria.
DR   eggNOG; COG4668; Bacteria.
DR   HOGENOM; CLU_046384_0_0_6; -.
DR   OMA; QGIEWGE; -.
DR   BioCyc; VCHO:VCA0518-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00367; PTS-HPr_like; 1.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   Gene3D; 3.30.1340.10; -; 1.
DR   Gene3D; 3.40.930.10; -; 1.
DR   InterPro; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_sf.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR001020; PTS_HPr_His_P_site.
DR   InterPro; IPR002114; PTS_HPr_Ser_P_site.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   PRINTS; PR00107; PHOSPHOCPHPR.
DR   SUPFAM; SSF55594; SSF55594; 1.
DR   SUPFAM; SSF55804; SSF55804; 2.
DR   TIGRFAMs; TIGR01003; PTS_HPr_family; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
DR   PROSITE; PS00369; PTS_HPR_HIS; 1.
DR   PROSITE; PS00589; PTS_HPR_SER; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transport.
FT   CHAIN           1..400
FT                   /note="Multiphosphoryl transfer protein"
FT                   /id="PRO_0000453370"
FT   DOMAIN          2..142
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   DOMAIN          310..400
FT                   /note="HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT   ACT_SITE        62
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   ACT_SITE        324
FT                   /note="Pros-phosphohistidine intermediate; for HPr
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT   MOD_RES         62
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P69811"
FT   MOD_RES         324
FT                   /note="Phosphohistidine; by EI"
FT                   /evidence="ECO:0000250|UniProtKB:P69811"
SQ   SEQUENCE   400 AA;  42614 MW;  4B34979C6AAB18F7 CRC64;
     MLELTTQDIQ LQQHFANKQA AIQGLAHALT AKGLVAEGYA QGMLNREAQH STYLGNGIAI
     PHGTTDTREL VKQTGVTAMH FPQGLDWGDG NLVYVAIGIA AKSDEHLGIL KQLTRVLSAD
     GVEQALQQAK TAQQIIAIIK GEAQLTADFD ASLIQLQFPA SDMVQMSAVA GGLLKNTGCA
     ENEFVADLVT KAPTHLGRGL WLVASDRAVK RTGMSIVTTA NHCEYEQQAV KALIAFSVCN
     DVHQPLLNTI TQCVFEQKQD QLLQADVQQL LNLFSGNAEQ TIAQRTIAVG TITEETIAAE
     TVAEPDSARA HTATFRIKNS HGLHARPGAM LVAEAKKFES NIRVSNLDGD GQVVNAKSLM
     KVIALGVKHN HQLQFTAEGP DAEAALQALG VAINAGLGEG