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Database: UniProt
Entry: A0A101WH23_9FIRM
LinkDB: A0A101WH23_9FIRM
Original site: A0A101WH23_9FIRM 
ID   A0A101WH23_9FIRM        Unreviewed;        88 AA.
AC   A0A101WH23;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Phosphocarrier protein HPr {ECO:0000256|ARBA:ARBA00020422};
GN   ORFNames=APF77_09790 {ECO:0000313|EMBL:KUO72971.1};
OS   Clostridia bacterium BRH_c25.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO72971.1, ECO:0000313|Proteomes:UP000057710};
RN   [1] {ECO:0000313|EMBL:KUO72971.1, ECO:0000313|Proteomes:UP000057710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO72971.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUO72971.1}.
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DR   EMBL; LOES01000137; KUO72971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101WH23; -.
DR   STRING; 1734399.APF77_09790; -.
DR   Proteomes; UP000057710; 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:SF2; PHOSPHOCARRIER PROTEIN NPR; 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}.
FT   DOMAIN          1..88
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   88 AA;  9412 MW;  7C2E6A1AC97FB490 CRC64;
     MKKSIVIVNS ACGLHARPAS MLVSTAMKFS SDIIIKKNDK TANCKSILSV LSIGASNGDE
     LEIVIEGQDE ADAFNTIKDL FDLRIANA
//
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