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Entry: I7KGZ7_9LACO
LinkDB: I7KGZ7_9LACO
Original site: I7KGZ7_9LACO 
ID   I7KGZ7_9LACO            Unreviewed;        88 AA.
AC   I7KGZ7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Phosphocarrier protein HPr {ECO:0000256|ARBA:ARBA00020422};
GN   ORFNames=BN55_09845 {ECO:0000313|EMBL:CCI81695.1};
OS   Lactobacillus hominis DSM 23910 = CRBIP 24.179.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423758 {ECO:0000313|EMBL:CCI81695.1, ECO:0000313|Proteomes:UP000009320};
RN   [1] {ECO:0000313|EMBL:CCI81695.1, ECO:0000313|Proteomes:UP000009320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRBIP 24.179T {ECO:0000313|Proteomes:UP000009320};
RA   Cousin S., Ma L., Bizet C., Loux V., Bouchier C., Clermont D., Creno S.;
RT   "Draft Genome Sequence of Lactobacillus hominis Strain CRBIP 24.179T,
RT   isolated from human intestine.";
RL   Submitted (JUN-2012) 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:CCI81695.1}.
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DR   EMBL; CAKE01000007; CCI81695.1; -; Genomic_DNA.
DR   RefSeq; WP_008470550.1; NZ_CAKE01000007.1.
DR   AlphaFoldDB; I7KGZ7; -.
DR   STRING; 1423758.FC41_GL000749; -.
DR   GeneID; 82846934; -.
DR   PATRIC; fig|1423758.3.peg.756; -.
DR   eggNOG; COG1925; Bacteria.
DR   OrthoDB; 9809047at2; -.
DR   Proteomes; UP000009320; 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;  9364 MW;  0CF153F710EFFD24 CRC64;
     MEKREFHIIA ETGIHARPAT LLVQTASKFN SDINLEYNGK SVNLKSIMGV MSLGVGQGAD
     VTITADGDDA KEAIDAIADT MKKEGLAE
//
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