PSTC_ECOLI
ID PSTC_ECOLI Reviewed; 319 AA.
AC P0AGH8; P07653; Q2M845;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphate transport system permease protein PstC;
GN Name=pstC; Synonyms=phoW; OrderedLocusNames=b3727, JW3705;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2993631; DOI=10.1016/0022-2836(85)90377-8;
RA Amemura M., Makino K., Shinagawa H., Kobayashi A., Nakata A.;
RT "Nucleotide sequence of the genes involved in phosphate transport and
RT regulation of the phosphate regulon in Escherichia coli.";
RL J. Mol. Biol. 184:241-250(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3881386; DOI=10.1128/jb.161.1.189-198.1985;
RA Surin B.P., Rosenberg H., Cox G.B.;
RT "Phosphate-specific transport system of Escherichia coli: nucleotide
RT sequence and gene-polypeptide relationships.";
RL J. Bacteriol. 161:189-198(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP MUTAGENESIS.
RX PubMed=1447208; DOI=10.1016/s0021-9258(18)35815-0;
RA Webb D.C., Rosenberg H., Cox G.B.;
RT "Mutational analysis of the Escherichia coli phosphate-specific transport
RT system, a member of the traffic ATPase (or ABC) family of membrane
RT transporters. A role for proline residues in transmembrane helices.";
RL J. Biol. Chem. 267:24661-24668(1992).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC phosphate; probably responsible for the translocation of the substrate
CC across the membrane.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; X02723; CAA26507.1; -; Genomic_DNA.
DR EMBL; K01992; AAA24379.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62078.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76750.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77561.1; -; Genomic_DNA.
DR PIR; H65175; BVECPW.
DR RefSeq; NP_418183.1; NC_000913.3.
DR RefSeq; WP_000741620.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P0AGH8; -.
DR BioGRID; 4262140; 41.
DR ComplexPortal; CPX-4381; Phosphate ABC transporter complex.
DR STRING; 511145.b3727; -.
DR TCDB; 3.A.1.7.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0AGH8; -.
DR PRIDE; P0AGH8; -.
DR EnsemblBacteria; AAC76750; AAC76750; b3727.
DR EnsemblBacteria; BAE77561; BAE77561; BAE77561.
DR GeneID; 66672373; -.
DR GeneID; 948238; -.
DR KEGG; ecj:JW3705; -.
DR KEGG; eco:b3727; -.
DR PATRIC; fig|1411691.4.peg.2973; -.
DR EchoBASE; EB0777; -.
DR eggNOG; COG0573; Bacteria.
DR HOGENOM; CLU_033621_1_3_6; -.
DR InParanoid; P0AGH8; -.
DR OMA; VIRMSVL; -.
DR PhylomeDB; P0AGH8; -.
DR BioCyc; EcoCyc:PSTC-MON; -.
DR BioCyc; MetaCyc:PSTC-MON; -.
DR PRO; PR:P0AGH8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IMP:EcoCyc.
DR GO; GO:0010921; P:regulation of phosphatase activity; IDA:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR011864; Phosphate_PstC.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR02138; phosphate_pstC; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Phosphate transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..319
FT /note="Phosphate transport system permease protein PstC"
FT /id="PRO_0000060207"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 45..74
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 95..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 138..167
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 188..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..252
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 253..283
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 304..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 75..305
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 319 AA; 34121 MW; 843F9E811DB62597 CRC64;
MAATKPAFNP PGKKGDIIFS VLVKLAALIV LLMLGGIIVS LIISSWPSIQ KFGLAFLWTK
EWDAPNDIYG ALVPIYGTLV TSFIALLIAV PVSFGIALFL TELAPGWLKR PLGIAIELLA
AIPSIVYGMW GLFIFAPLFA VYFQEPVGNI MSNIPIVGAL FSGPAFGIGI LAAGVILAIM
IIPYIAAVMR DVFEQTPVMM KESAYGIGCT TWEVIWRIVL PFTKNGVIGG IMLGLGRALG
ETMAVTFIIG NTYQLDSASL YMPGNSITSA LANEFAEAES GLHVAALMEL GLILFVITFI
VLAASKFMIM RLAKNEGAR
