ID PTHP_LISMO Reviewed; 88 AA.
AC P0A438; O31148;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Phosphocarrier protein HPr;
DE AltName: Full=Histidine-containing protein;
GN Name=ptsH; OrderedLocusNames=lmo1002;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Scott A;
RX PubMed=9726852; DOI=10.1128/aem.64.9.3147-3152.1998;
RA Christensen D.P., Benson A.K., Hutkins R.W.;
RT "Cloning and expression of the Listeria monocytogenes Scott A ptsH and ptsI
RT genes, coding for HPr and enzyme I, respectively, of the phosphotransferase
RT system.";
RL Appl. Environ. Microbiol. 64:3147-3152(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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.
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 (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Phosphorylation on Ser-46 inhibits the phosphoryl
CC transfer from enzyme I to HPr. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR EMBL; AF030824; AAC36127.1; -; Genomic_DNA.
DR EMBL; AL591977; CAC99080.1; -; Genomic_DNA.
DR PIR; AB1200; AB1200.
DR RefSeq; NP_464527.1; NC_003210.1.
DR RefSeq; WP_003719221.1; NZ_CP023861.1.
DR AlphaFoldDB; P0A438; -.
DR SMR; P0A438; -.
DR STRING; 169963.gene:17593658; -.
DR PaxDb; 169963-lmo1002; -.
DR EnsemblBacteria; CAC99080; CAC99080; CAC99080.
DR GeneID; 84561591; -.
DR GeneID; 986517; -.
DR KEGG; lmo:lmo1002; -.
DR PATRIC; fig|169963.11.peg.1030; -.
DR eggNOG; COG1925; Bacteria.
DR HOGENOM; CLU_136230_2_2_9; -.
DR OrthoDB; 9809047at2; -.
DR PhylomeDB; P0A438; -.
DR BioCyc; LMON169963:LMO1002-MONOMER; -.
DR Proteomes; UP000000817; 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; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transcription; Transcription regulation; Transport.
FT CHAIN 1..88
FT /note="Phosphocarrier protein HPr"
FT /id="PRO_0000107861"
FT DOMAIN 1..88
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 15
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT MOD_RES 46
FT /note="Phosphoserine; by HPrK/P"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
SQ SEQUENCE 88 AA; 9404 MW; 81B5A4E95CCA3BF4 CRC64;
MEQASFVVID ETGIHARPAT LLVQAASKYS SDVQIEYTGK KVNLKSIMGV MSLGIGKGAD
ITIYTEGSDE KEAIEGLTEV LKKEGLAE
//
