PSTA_ECOLI
ID PSTA_ECOLI Reviewed; 296 AA.
AC P07654; Q2M844;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Phosphate transport system permease protein PstA;
GN Name=pstA; Synonyms=phoT; OrderedLocusNames=b3726, JW3704;
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.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11867724; DOI=10.1073/pnas.052018199;
RA Drew D., Sjoestrand D., Nilsson J., Urbig T., Chin C.-N., de Gier J.-W.,
RA von Heijne G.;
RT "Rapid topology mapping of Escherichia coli inner-membrane proteins by
RT prediction and PhoA/GFP fusion analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2690-2695(2002).
RN [8]
RP SUBCELLULAR LOCATION.
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
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X02723; CAA26508.1; -; Genomic_DNA.
DR EMBL; K01992; AAA24380.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62077.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76749.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77562.1; -; Genomic_DNA.
DR PIR; B23311; BVECPT.
DR RefSeq; NP_418182.1; NC_000913.3.
DR RefSeq; WP_001251998.1; NZ_SSZK01000036.1.
DR AlphaFoldDB; P07654; -.
DR SMR; P07654; -.
DR BioGRID; 4262142; 12.
DR ComplexPortal; CPX-4381; Phosphate ABC transporter complex.
DR STRING; 511145.b3726; -.
DR TCDB; 3.A.1.7.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P07654; -.
DR PRIDE; P07654; -.
DR EnsemblBacteria; AAC76749; AAC76749; b3726.
DR EnsemblBacteria; BAE77562; BAE77562; BAE77562.
DR GeneID; 948239; -.
DR KEGG; ecj:JW3704; -.
DR KEGG; eco:b3726; -.
DR PATRIC; fig|1411691.4.peg.2974; -.
DR EchoBASE; EB0775; -.
DR eggNOG; COG0581; Bacteria.
DR HOGENOM; CLU_033621_2_0_6; -.
DR InParanoid; P07654; -.
DR OMA; GIARWKA; -.
DR PhylomeDB; P07654; -.
DR BioCyc; EcoCyc:PSTA-MON; -.
DR BioCyc; MetaCyc:MON-21699; -.
DR BioCyc; MetaCyc:PSTA-MON; -.
DR PRO; PR:P07654; -.
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; IDA:EcoliWiki.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006817; P:phosphate ion transport; IDA:EcoCyc.
DR GO; GO:0010921; P:regulation of phosphatase activity; IDA: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; IPR005672; Phosphate_PstA.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR00974; 3a0107s02c; 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..296
FT /note="Phosphate transport system permease protein PstA"
FT /id="PRO_0000060193"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 51..82
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 103..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 147..150
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..169
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 170..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 224..266
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..286
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 287..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 83..286
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 296 AA; 32322 MW; BFEADEC0B9851DC7 CRC64;
MAMVEMQTTA ALAESRRKMQ ARRRLKNRIA LTLSMATMAF GLFWLIWILM STITRGIDGM
SLALFTEMTP PPNTEGGGLA NALAGSGLLI LWATVFGTPL GIMAGIYLAE YGRKSWLAEV
IRFINDILLS APSIVVGLFV YTIVVAQMEH FSGWAGVIAL ALLQVPIVIR TTENMLKLVP
YSLREAAYAL GTPKWKMISA ITLKASVSGI MTGILLAIAR IAGETAPLLF TALSNQFWST
DMMQPIANLP VTIFKFAMSP FAEWQQLAWA GVLIITLCVL LLNILARVVF AKNKHG
