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Database: UniProt
Entry: A0A1G8E8G7_9VIBR
LinkDB: A0A1G8E8G7_9VIBR
Original site: A0A1G8E8G7_9VIBR 
ID   A0A1G8E8G7_9VIBR        Unreviewed;        85 AA.
AC   A0A1G8E8G7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Phosphocarrier protein HPr {ECO:0000256|ARBA:ARBA00020422};
DE   AltName: Full=Histidine-containing protein {ECO:0000256|ARBA:ARBA00033055};
GN   ORFNames=SAMN04488136_12360 {ECO:0000313|EMBL:SDH66232.1};
OS   Vibrio xiamenensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=861298 {ECO:0000313|EMBL:SDH66232.1, ECO:0000313|Proteomes:UP000198854};
RN   [1] {ECO:0000313|EMBL:SDH66232.1, ECO:0000313|Proteomes:UP000198854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10228 {ECO:0000313|EMBL:SDH66232.1,
RC   ECO:0000313|Proteomes:UP000198854};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00003681}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; FNDD01000023; SDH66232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8E8G7; -.
DR   STRING; 861298.SAMN04488136_12360; -.
DR   OrthoDB; 9809047at2; -.
DR   Proteomes; UP000198854; 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; HPr-like; 1.
DR   InterPro; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_sf.
DR   InterPro; IPR001020; PTS_HPr_His_P_site.
DR   InterPro; IPR002114; PTS_HPr_Ser_P_site.
DR   NCBIfam; TIGR01003; PTS_HPr_family; 1.
DR   PANTHER; PTHR33705; PHOSPHOCARRIER PROTEIN HPR; 1.
DR   PANTHER; PTHR33705:SF1; PHOSPHOCARRIER PROTEIN HPR; 1.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   PRINTS; PR00107; PHOSPHOCPHPR.
DR   SUPFAM; SSF55594; HPr-like; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
DR   PROSITE; PS00369; PTS_HPR_HIS; 1.
DR   PROSITE; PS00589; PTS_HPR_SER; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198854};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..85
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   85 AA;  9166 MW;  A4BF25BFC68B6C60 CRC64;
     MYEKQVEITA ENGLHTRPAA QFVKEAKAFD ADITVTSNGK SASAKSLFKL QTLGLVKGTL
     VTISAEGPQA QQAVDHLVEL MDQLH
//
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