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Database: UniProt
Entry: A0A1H6TMZ0_9LACT
LinkDB: A0A1H6TMZ0_9LACT
Original site: A0A1H6TMZ0_9LACT 
ID   A0A1H6TMZ0_9LACT        Unreviewed;        88 AA.
AC   A0A1H6TMZ0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Phosphocarrier protein HPr {ECO:0000256|ARBA:ARBA00020422};
GN   ORFNames=SAMN04488113_1193 {ECO:0000313|EMBL:SEI77610.1};
OS   Alkalibacterium gilvum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=1130080 {ECO:0000313|EMBL:SEI77610.1, ECO:0000313|Proteomes:UP000198564};
RN   [1] {ECO:0000313|Proteomes:UP000198564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25751 {ECO:0000313|Proteomes:UP000198564};
RA   Varghese N., Submissions S.;
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   -!- FUNCTION: P-Ser-HPr interacts with the catabolite control protein A
CC       (CcpA), forming a complex that binds to DNA at the catabolite response
CC       elements cre, operator sites preceding a large number of catabolite-
CC       regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite
CC       repression (CCR), a mechanism that allows bacteria to coordinate and
CC       optimize the utilization of available carbon sources. P-Ser-HPr also
CC       plays a role in inducer exclusion, in which it probably interacts with
CC       several non-PTS permeases and inhibits their transport activity.
CC       {ECO:0000256|ARBA:ARBA00024781}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the HPr family. {ECO:0000256|ARBA:ARBA00010736}.
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DR   EMBL; FNYW01000019; SEI77610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6TMZ0; -.
DR   STRING; 1130080.SAMN04488113_1193; -.
DR   OrthoDB; 9809047at2; -.
DR   Proteomes; UP000198564; 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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..88
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   88 AA;  9344 MW;  5FC6BD9AFEDEB753 CRC64;
     MEKREYTIIA DTGIHARPAT LLVQQASKFN SDITLEYKGK SVNLKSIMGV MSLGVGKGAE
     VTITADGADE KDAIEGIDGT IKNEGMAE
//
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