ID A0A1I1EAY4_9LACT Unreviewed; 88 AA.
AC A0A1I1EAY4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phosphocarrier protein HPr {ECO:0000256|ARBA:ARBA00020422};
GN ORFNames=SAMN04488102_10177 {ECO:0000313|EMBL:SFB84289.1};
OS Alkalibacterium subtropicum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=753702 {ECO:0000313|EMBL:SFB84289.1, ECO:0000313|Proteomes:UP000199612};
RN [1] {ECO:0000313|EMBL:SFB84289.1, ECO:0000313|Proteomes:UP000199612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23664 {ECO:0000313|EMBL:SFB84289.1,
RC ECO:0000313|Proteomes:UP000199612};
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 -!- 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; FOLT01000001; SFB84289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1EAY4; -.
DR STRING; 753702.SAMN04488102_10177; -.
DR OrthoDB; 9809047at2; -.
DR Proteomes; UP000199612; 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; 9416 MW; 1F1F41AF88186C3F CRC64;
MEKREYTIIA DTGIHARPAT LLVQQASKFN SDITLDYKGK SVNLKSIMGV MSLGVGKGAE
VSITADGADE KEAIEGIEET IKNEGMAE
//