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   03-AUG-2022, entry version 111.
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; Firmicutes; 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.lmo1002; -.
DR   PaxDb; P0A438; -.
DR   EnsemblBacteria; CAC99080; CAC99080; CAC99080.
DR   GeneID; 61188876; -.
DR   GeneID; 67409302; -.
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   OMA; SIMAMMM; -.
DR   PhylomeDB; P0A438; -.
DR   BioCyc; LMON169963:LMO1002-MON; -.
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; -; 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   Pfam; PF00381; PTS-HPr; 1.
DR   PRINTS; PR00107; PHOSPHOCPHPR.
DR   SUPFAM; SSF55594; SSF55594; 1.
DR   TIGRFAMs; TIGR01003; PTS_HPr_family; 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