ID   PTHP_HALVD              Reviewed;          89 AA.
AC   D4GYE3;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Phosphocarrier protein HPr;
GN   Name=ptsH1; OrderedLocusNames=HVO_1497; ORFNames=C498_11246;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [3]
RP   IDENTIFICATION, FUNCTION, AND INDUCTION.
RC   STRAIN=DS2 / DS70;
RX   PubMed=22493022; DOI=10.1128/jb.00200-12;
RA   Pickl A., Johnsen U., Schoenheit P.;
RT   "Fructose degradation in the haloarchaeon Haloferax volcanii involves a
RT   bacterial type phosphoenolpyruvate-dependent phosphotransferase system,
RT   fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate
RT   aldolase.";
RL   J. Bacteriol. 194:3088-3097(2012).
CC   -!- FUNCTION: General (non sugar-specific) component of the
CC       phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar
CC       PTS). This major carbohydrate active-transport system catalyzes the
CC       phosphorylation of incoming sugar substrates concomitantly with their
CC       translocation across the cell membrane. The phosphoryl group from
CC       phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier
CC       protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA
CC       domain (By similarity). Is involved in fructose transport.
CC       {ECO:0000250, ECO:0000269|PubMed:22493022}.
CC   -!- ACTIVITY REGULATION: Phosphorylation on Ser-47 inhibits the phosphoryl
CC       transfer from enzyme I to HPr. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Expression is highly up-regulated in presence of fructose.
CC       {ECO:0000269|PubMed:22493022}.
CC   -!- MISCELLANEOUS: PTS-type transport systems are very rare in archaea.
CC   -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR   EMBL; CP001956; ADE03675.1; -; Genomic_DNA.
DR   EMBL; AOHU01000090; ELY28265.1; -; Genomic_DNA.
DR   RefSeq; WP_004043438.1; NZ_AOHU01000090.1.
DR   AlphaFoldDB; D4GYE3; -.
DR   SMR; D4GYE3; -.
DR   STRING; 309800.C498_11246; -.
DR   TCDB; 8.A.8.1.4; the phosphotransferase system hpr (hpr) family.
DR   EnsemblBacteria; ADE03675; ADE03675; HVO_1497.
DR   EnsemblBacteria; ELY28265; ELY28265; C498_11246.
DR   GeneID; 8925514; -.
DR   KEGG; hvo:HVO_1497; -.
DR   PATRIC; fig|309800.29.peg.2143; -.
DR   eggNOG; arCOG04543; Archaea.
DR   HOGENOM; CLU_136230_1_1_2; -.
DR   OMA; RRVNVGW; -.
DR   OrthoDB; 124925at2157; -.
DR   Proteomes; UP000008243; Chromosome.
DR   Proteomes; UP000011532; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd00367; PTS-HPr_like; 1.
DR   Gene3D; 3.30.1340.10; -; 1.
DR   InterPro; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_sf.
DR   InterPro; IPR001020; PTS_HPr_His_P_site.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   PRINTS; PR00107; PHOSPHOCPHPR.
DR   SUPFAM; SSF55594; SSF55594; 1.
DR   TIGRFAMs; TIGR01003; PTS_HPr_family; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
DR   PROSITE; PS00369; PTS_HPR_HIS; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transport.
FT   CHAIN           1..89
FT                   /note="Phosphocarrier protein HPr"
FT                   /id="PRO_0000428986"
FT   DOMAIN          1..89
FT                   /note="HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT   ACT_SITE        14
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT   MOD_RES         47
FT                   /note="Phosphoserine; by HPrK/P"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
SQ   SEQUENCE   89 AA;  9359 MW;  7A0B355161D7117E CRC64;
     MERTVTVVPE DGLHARPASK FVETANKFDA DVQLGRADED DLVPAASMLA VTGLGVGHDE
     SVRLVAEGDD AEAALDALED ILSTPEAKQ