PTSO_PROMH
ID PTSO_PROMH Reviewed; 90 AA.
AC Q9ZA86; B4EX43;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Phosphocarrier protein NPr;
DE AltName: Full=Nitrogen-related HPr;
GN Name=ptsO; OrderedLocusNames=PMI3644;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10206698; DOI=10.1099/13500872-145-1-185;
RA Zhao H., Li X., Johnson D.E., Mobley H.L.T.;
RT "Identification of protease and rpoN-associated genes of uropathogenic
RT Proteus mirabilis by negative selection in a mouse model of ascending
RT urinary tract infection.";
RL Microbiology 145:185-195(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
CC -!- FUNCTION: Component of the phosphoenolpyruvate-dependent nitrogen-
CC metabolic phosphotransferase system (nitrogen-metabolic PTS), that
CC seems to be involved in regulating nitrogen metabolism. The phosphoryl
CC group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl
CC carrier protein NPr by enzyme I-Ntr. Phospho-NPr then transfers it to
CC EIIA-Ntr. Could function in the transcriptional regulation of sigma-54
CC dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr
CC (PtsN) proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}.
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DR EMBL; AF088980; AAC64576.1; -; Genomic_DNA.
DR EMBL; AM942759; CAR47115.1; -; Genomic_DNA.
DR RefSeq; WP_004245309.1; NC_010554.1.
DR AlphaFoldDB; Q9ZA86; -.
DR SMR; Q9ZA86; -.
DR STRING; 529507.PMI3644; -.
DR EnsemblBacteria; CAR47115; CAR47115; PMI3644.
DR GeneID; 6800963; -.
DR KEGG; pmr:PMI3644; -.
DR eggNOG; COG1925; Bacteria.
DR HOGENOM; CLU_136230_1_3_6; -.
DR OMA; HARPAMM; -.
DR Proteomes; UP000008319; 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; Phosphotransferase system; Reference proteome.
FT CHAIN 1..90
FT /note="Phosphocarrier protein NPr"
FT /id="PRO_0000107894"
FT DOMAIN 2..90
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 16
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT CONFLICT 28
FT /note="N -> H (in Ref. 1; AAC64576)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..66
FT /note="IE -> MK (in Ref. 1; AAC64576)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="A -> T (in Ref. 1; AAC64576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 90 AA; 10014 MW; 8E13F66943C5A2FF CRC64;
MTQYRRVAIK NRLGMHARPA MKLFDLVNTF QSTVTLRNHE GVEAQADSVI AMLMLDSEQG
SHIDIEASGC DEKEAIDAII ALFESGFDED