ACTP_ECOLI
ID ACTP_ECOLI Reviewed; 549 AA.
AC P32705; Q2M6N7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Cation/acetate symporter ActP;
DE AltName: Full=Acetate permease;
DE AltName: Full=Acetate transporter ActP;
GN Name=actP; Synonyms=yjcG; OrderedLocusNames=b4067, JW4028;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12;
RX PubMed=14563880; DOI=10.1128/jb.185.21.6448-6455.2003;
RA Gimenez R., Nunez M.F., Badia J., Aguilar J., Baldoma L.;
RT "The gene yjcG, cotranscribed with the gene acs, encodes an acetate
RT permease in Escherichia coli.";
RL J. Bacteriol. 185:6448-6455(2003).
RN [5]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [6]
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: Transports acetate. Also able to transport glycolate.
CC {ECO:0000269|PubMed:14563880}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 uM for acetate {ECO:0000269|PubMed:14563880};
CC Vmax=19.6 nmol/min/mg enzyme {ECO:0000269|PubMed:14563880};
CC -!- SUBUNIT: Has been isolated from inner membrane preparations as a
CC homodimer. {ECO:0000269|PubMed:16079137}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16079137}.
CC -!- MISCELLANEOUS: Although ActP belongs to the sodium:solute symporter
CC family, the experiments did not allow to show that acetate transport
CC depends on sodium. The inhibition of acetate transport by the uncoupler
CC CCCP indicates that the driving force used by ActP is a transmembrane
CC electrochemical potential. However, it does not allow to discriminate
CC between hydrogen ion or sodium ion-coupled transporters
CC (PubMed:14563880). {ECO:0000305|PubMed:14563880}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
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DR EMBL; U00006; AAC43161.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77037.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78069.1; -; Genomic_DNA.
DR PIR; B65215; B65215.
DR RefSeq; NP_418491.1; NC_000913.3.
DR RefSeq; WP_000832573.1; NZ_SSZK01000016.1.
DR AlphaFoldDB; P32705; -.
DR SMR; P32705; -.
DR BioGRID; 4259431; 12.
DR DIP; DIP-12552N; -.
DR IntAct; P32705; 1.
DR STRING; 511145.b4067; -.
DR TCDB; 2.A.21.7.2; the solute:sodium symporter (sss) family.
DR jPOST; P32705; -.
DR PaxDb; P32705; -.
DR PRIDE; P32705; -.
DR EnsemblBacteria; AAC77037; AAC77037; b4067.
DR EnsemblBacteria; BAE78069; BAE78069; BAE78069.
DR GeneID; 948575; -.
DR KEGG; ecj:JW4028; -.
DR KEGG; eco:b4067; -.
DR PATRIC; fig|1411691.4.peg.2637; -.
DR EchoBASE; EB1886; -.
DR eggNOG; COG4147; Bacteria.
DR HOGENOM; CLU_018808_8_3_6; -.
DR InParanoid; P32705; -.
DR OMA; GTTWVQM; -.
DR PhylomeDB; P32705; -.
DR BioCyc; EcoCyc:YJCG-MON; -.
DR BioCyc; MetaCyc:YJCG-MON; -.
DR PRO; PR:P32705; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015123; F:acetate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0043879; F:glycolate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015654; F:tellurite transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0006847; P:plasma membrane acetate transport; IDA:EcoCyc.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0015710; P:tellurite transport; IMP:EcoCyc.
DR Gene3D; 1.20.1730.10; -; 1.
DR HAMAP; MF_01426; Acet_symport_ActP; 1.
DR InterPro; IPR014083; Cation/Ac_symporter_ActP.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR018212; Na/solute_symporter_CS.
DR Pfam; PF00474; SSF; 1.
DR TIGRFAMs; TIGR00813; sss; 1.
DR TIGRFAMs; TIGR02711; symport_actP; 1.
DR PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
DR PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..549
FT /note="Cation/acetate symporter ActP"
FT /id="PRO_0000105407"
FT TOPO_DOM 1..32
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..102
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..182
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..260
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..358
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..427
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..493
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 549 AA; 59197 MW; E7E116FB919D0FFD CRC64;
MKRVLTALAA TLPFAANAAD AISGAVERQP TNWQAIIMFL IFVVFTLGIT YWASKRVRSR
SDYYTAGGNI TGFQNGLAIA GDYMSAASFL GISALVFTSG YDGLIYSLGF LVGWPIILFL
IAERLRNLGR YTFADVASYR LKQGPIRILS ACGSLVVVAL YLIAQMVGAG KLIELLFGLN
YHIAVVLVGV LMMMYVLFGG MLATTWVQII KAVLLLFGAS FMAFMVMKHV GFSFNNLFSE
AMAVHPKGVD IMKPGGLVKD PISALSLGLG LMFGTAGLPH ILMRFFTVSD AREARKSVFY
ATGFMGYFYI LTFIIGFGAI MLVGANPEYK DAAGHLIGGN NMAAVHLANA VGGNLFLGFI
SAVAFATILA VVAGLTLAGA SAVSHDLYAN VFKKGATERE ELRVSKITVL ILGVIAIILG
VLFENQNIAF MVGLAFAIAA SCNFPIILLS MYWSKLTTRG AMMGGWLGLI TAVVLMILGP
TIWVQILGHE KAIFPYEYPA LFSITVAFLG IWFFSATDNS AEGARERELF RAQFIRSQTG
FGVEQGRAH
