ID A0A062X4T8_9LACO Unreviewed; 88 AA.
AC A0A062X4T8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Phosphocarrier protein HPr {ECO:0000256|ARBA:ARBA00020422};
GN ORFNames=Lani381_1105 {ECO:0000313|EMBL:KDA45778.1};
OS Ligilactobacillus animalis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1605 {ECO:0000313|EMBL:KDA45778.1, ECO:0000313|Proteomes:UP000027129};
RN [1] {ECO:0000313|EMBL:KDA45778.1, ECO:0000313|Proteomes:UP000027129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=381-IL-28 {ECO:0000313|EMBL:KDA45778.1,
RC ECO:0000313|Proteomes:UP000027129};
RA Sturino J.M., Rajendran M., Altermann E.;
RT "Draft Genome Sequence of Lactobacillus animalis 381-IL-28.";
RL Submitted (APR-2014) 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}.
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:KDA45778.1}.
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DR EMBL; JMHU01000009; KDA45778.1; -; Genomic_DNA.
DR RefSeq; WP_010688426.1; NZ_POVP01000007.1.
DR AlphaFoldDB; A0A062X4T8; -.
DR GeneID; 61225995; -.
DR PATRIC; fig|1605.9.peg.1083; -.
DR eggNOG; COG1925; Bacteria.
DR OrthoDB; 9809047at2; -.
DR Proteomes; UP000027129; 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}.
SQ SEQUENCE 88 AA; 9264 MW; 87B53D7A81E55105 CRC64;
MEKKEFHVIA ETGIHARPAT LLVQAASKFN SDITLEYQGK SVNLKSIMGV MSLGVGQNAD
VVISADGADE AEAIAAITET MTKEGLAE
//
