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Entry: A0A1L4BZ51_9LACT
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ID   A0A1L4BZ51_9LACT        Unreviewed;        88 AA.
AC   A0A1L4BZ51;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Phosphocarrier protein HPr {ECO:0000256|ARBA:ARBA00020422};
GN   ORFNames=BKP56_07620 {ECO:0000313|EMBL:API89128.1};
OS   Marinilactibacillus sp. 15R.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Marinilactibacillus.
OX   NCBI_TaxID=1911586 {ECO:0000313|EMBL:API89128.1, ECO:0000313|Proteomes:UP000184433};
RN   [1] {ECO:0000313|EMBL:API89128.1, ECO:0000313|Proteomes:UP000184433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=15R {ECO:0000313|EMBL:API89128.1,
RC   ECO:0000313|Proteomes:UP000184433};
RA   Wei Y., Cao J., Fang J.;
RT   "Genome sequence of Marinilactibacillus sp. 15R.";
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; CP017761; API89128.1; -; Genomic_DNA.
DR   RefSeq; WP_072694521.1; NZ_CP017761.1.
DR   AlphaFoldDB; A0A1L4BZ51; -.
DR   STRING; 1911586.BKP56_07620; -.
DR   KEGG; marr:BKP56_07620; -.
DR   Proteomes; UP000184433; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000184433};
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;  9349 MW;  AF7F06BD05C5AFC3 CRC64;
     MEKRSYNVTA ETGIHARPAT LLVQTASKYN SDITLEYKGK SVNLKSIMGV MSLGVGQGAD
     VTISAEGADE TEAIEGIEQT IKNEGMAE
//
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