PITA_ECO57
ID PITA_ECO57 Reviewed; 499 AA.
AC P0AFJ9; P37308;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Low-affinity inorganic phosphate transporter 1;
GN Name=pitA; OrderedLocusNames=Z4893, ECs4365;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Low-affinity inorganic phosphate transport. Can also
CC transport arsenate (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC
CC 2.A.20) family. Pit subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG58625.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37788.1; -; Genomic_DNA.
DR PIR; E86020; E86020.
DR PIR; E91174; E91174.
DR RefSeq; NP_312392.1; NC_002695.1.
DR RefSeq; WP_000902780.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AFJ9; -.
DR SMR; P0AFJ9; -.
DR STRING; 155864.EDL933_4730; -.
DR PRIDE; P0AFJ9; -.
DR EnsemblBacteria; AAG58625; AAG58625; Z4893.
DR EnsemblBacteria; BAB37788; BAB37788; ECs_4365.
DR GeneID; 66672625; -.
DR GeneID; 913986; -.
DR KEGG; ece:Z4893; -.
DR KEGG; ecs:ECs_4365; -.
DR PATRIC; fig|386585.9.peg.4559; -.
DR eggNOG; COG0306; Bacteria.
DR HOGENOM; CLU_015355_4_0_6; -.
DR OMA; GYDITRT; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR001204; Phos_transporter.
DR PANTHER; PTHR11101; PTHR11101; 1.
DR Pfam; PF01384; PHO4; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Phosphate transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..499
FT /note="Low-affinity inorganic phosphate transporter 1"
FT /id="PRO_0000080783"
FT TOPO_DOM 1..4
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..93
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..154
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..232
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..429
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..499
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 499 AA; 53389 MW; 93D551131C524084 CRC64;
MLHLFAGLDL HTGLLLLLAL AFVLFYEAIN GFHDTANAVA TVIYTRAMRS QLAVVMAAVF
NFLGVLLGGL SVAYAIVHML PTDLLLNMGS SHGLAMVFSM LLAAIIWNLG TWYFGLPASS
SHTLIGAIIG IGLTNALMTG TSVVDALNIP KVLSIFGSLI VSPIVGLVFA GGLIFLLRRY
WSGTKKRARI HLTPAEREKK DGKKKPPFWT RIALILSAIG VAFSHGANDG QKGIGLVMLV
LIGVAPAGFV VNMNATGYEI TRTRDAINNV EAYFEQHPAL LKQATGADQL VPAPEAGATQ
PAEFHCHPSN TINALNRLKG MLTTDVESYD KLSLDQRSQM RRIMLCVSDT IDKVVKMPGV
SADDQRLLKK LKSDMLSTIE YAPVWIIMAV ALALGIGTMI GWRRVATTIG EKIGKKGMTY
AQGMSAQMTA AVSIGLASYT GMPVSTTHVL SSSVAGTMVV DGGGLQRKTV TSILMAWVFT
LPAAVLLSGG LYWLSLQFL
