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Database: UniProt
Entry: R5EFQ9_9FIRM
LinkDB: R5EFQ9_9FIRM
Original site: R5EFQ9_9FIRM 
ID   R5EFQ9_9FIRM            Unreviewed;        86 AA.
AC   R5EFQ9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Phosphocarrier protein HPr {ECO:0000256|ARBA:ARBA00020422};
GN   ORFNames=BN466_00801 {ECO:0000313|EMBL:CCX90154.1};
OS   Firmicutes bacterium CAG:110.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263000 {ECO:0000313|EMBL:CCX90154.1, ECO:0000313|Proteomes:UP000018021};
RN   [1] {ECO:0000313|EMBL:CCX90154.1, ECO:0000313|Proteomes:UP000018021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:110 {ECO:0000313|Proteomes:UP000018021};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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   -!- 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:CCX90154.1}.
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DR   EMBL; CAXG010000083; CCX90154.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5EFQ9; -.
DR   Proteomes; UP000018021; Unassembled WGS sequence.
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; 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; PS00589; PTS_HPR_SER; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018021}.
FT   DOMAIN          1..86
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   86 AA;  9410 MW;  6D4C8E4D242358B0 CRC64;
     MFNKEVVVRC ESGLHNRQAT YFVQKANEFE SSIWLESGSR RMNAKSLLGI MSLGVVTGTT
     VTLSASGPDA EAAVNALDEL LQRDVY
//
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