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Database: UniProt
Entry: D6LDM1_9FUSO
LinkDB: D6LDM1_9FUSO
Original site: D6LDM1_9FUSO 
ID   D6LDM1_9FUSO            Unreviewed;        87 AA.
AC   D6LDM1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Phosphocarrier protein HPr {ECO:0000256|ARBA:ARBA00020422};
DE   AltName: Full=Histidine-containing protein {ECO:0000256|ARBA:ARBA00033055};
GN   ORFNames=HMPREF0400_02053 {ECO:0000313|EMBL:EFG29406.2};
OS   Fusobacterium periodonticum 1_1_41FAA.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=469621 {ECO:0000313|EMBL:EFG29406.2, ECO:0000313|Proteomes:UP000003964};
RN   [1] {ECO:0000313|EMBL:EFG29406.2, ECO:0000313|Proteomes:UP000003964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_1_41FAA {ECO:0000313|EMBL:EFG29406.2,
RC   ECO:0000313|Proteomes:UP000003964};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Mehta T.,
RA   Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Strauss J.C.,
RA   Ambrose C.E., Allen-Vercoe E., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusobacterium sp. 1_1_41FAA.";
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; GG770375; EFG29406.2; -; Genomic_DNA.
DR   RefSeq; WP_005973384.1; NZ_GG770375.1.
DR   AlphaFoldDB; D6LDM1; -.
DR   GeneID; 78419682; -.
DR   Proteomes; UP000003964; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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   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.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:EFG29406.2};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..87
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   87 AA;  9368 MW;  A4A6F72A8E580294 CRC64;
     MKSKTVEIVN ETGLHTRPGN EFVSLAKTFS SQISVENEAG TKVNGTSLLK LLSLGIKKGS
     KITVYADGED ENEAVDKLSS LLENLKD
//
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