SATP_ECOLI
ID SATP_ECOLI Reviewed; 188 AA.
AC P0AC98; P28695; Q8KMY2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Succinate-acetate/proton symporter SatP;
DE AltName: Full=Succinate-acetate transporter protein;
GN Name=satP; Synonyms=yaaH; OrderedLocusNames=b0010, JW0009;
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=8400364; DOI=10.3109/10425179309020832;
RA James R., Dean D.O., Debbage J.;
RT "Five open reading frames upstream of the dnaK gene of E. coli.";
RL DNA Seq. 3:327-332(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 111.
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 [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND 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).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, GENE NAME, AND MUTAGENESIS OF LEU-131 AND ALA-164.
RC STRAIN=K12 / MG1693;
RX PubMed=23844911; DOI=10.1042/bj20130412;
RA Sa-Pessoa J., Paiva S., Ribas D., Silva I.J., Viegas S.C., Arraiano C.M.,
RA Casal M.;
RT "SATP (YaaH), a succinate-acetate transporter protein in Escherichia
RT coli.";
RL Biochem. J. 454:585-595(2013).
CC -!- FUNCTION: Uptake of acetate and succinate. Transport is energetically
CC dependent on the protonmotive force. {ECO:0000269|PubMed:23844911}.
CC -!- ACTIVITY REGULATION: Transport is inhibited by the protonophore CCCP.
CC {ECO:0000269|PubMed:23844911}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.24 mM for acetic acid {ECO:0000269|PubMed:23844911};
CC KM=1.18 mM for succinic acid {ECO:0000269|PubMed:23844911};
CC Vmax=8.72 nmol/min/mg enzyme with acetic acid as substrate
CC {ECO:0000269|PubMed:23844911};
CC Vmax=10.05 nmol/min/mg enzyme with succinic acid as substrate
CC {ECO:0000269|PubMed:23844911};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:23844911};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows a partial reduction in acetate
CC uptake. {ECO:0000269|PubMed:23844911}.
CC -!- SIMILARITY: Belongs to the acetate uptake transporter (AceTr) (TC
CC 2.A.96) family. {ECO:0000305}.
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DR EMBL; X67700; CAA47931.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73121.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96588.2; -; Genomic_DNA.
DR PIR; E56688; E56688.
DR RefSeq; NP_414551.1; NC_000913.3.
DR RefSeq; WP_000528538.1; NZ_STEB01000033.1.
DR PDB; 5ZUG; X-ray; 2.80 A; A/B/C/D/E/F=1-188.
DR PDBsum; 5ZUG; -.
DR AlphaFoldDB; P0AC98; -.
DR SMR; P0AC98; -.
DR STRING; 511145.b0010; -.
DR TCDB; 2.A.96.1.1; the acetate uptake transporter (acetr) family.
DR PaxDb; P0AC98; -.
DR PRIDE; P0AC98; -.
DR EnsemblBacteria; AAC73121; AAC73121; b0010.
DR EnsemblBacteria; BAB96588; BAB96588; BAB96588.
DR GeneID; 67416090; -.
DR GeneID; 944792; -.
DR KEGG; ecj:JW0009; -.
DR KEGG; eco:b0010; -.
DR PATRIC; fig|511145.12.peg.9; -.
DR EchoBASE; EB1474; -.
DR eggNOG; COG1584; Bacteria.
DR HOGENOM; CLU_051062_3_0_6; -.
DR InParanoid; P0AC98; -.
DR OMA; WKKGNTF; -.
DR PhylomeDB; P0AC98; -.
DR BioCyc; EcoCyc:EG11512-MON; -.
DR BioCyc; MetaCyc:EG11512-MON; -.
DR PRO; PR:P0AC98; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015360; F:acetate:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0035433; P:acetate transmembrane transport; IMP:EcoCyc.
DR GO; GO:0071422; P:succinate transmembrane transport; IDA:EcoCyc.
DR InterPro; IPR000791; Gpr1/Fun34/SatP.
DR Pfam; PF01184; Gpr1_Fun34_YaaH; 1.
DR PROSITE; PS01114; GPR1_FUN34_YAAH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..188
FT /note="Succinate-acetate/proton symporter SatP"
FT /id="PRO_0000135703"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..97
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..148
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 131
FT /note="L->V: Acquires ability to transport lactic acid."
FT /evidence="ECO:0000269|PubMed:23844911"
FT MUTAGEN 164
FT /note="A->G: Acquires ability to transport lactic acid."
FT /evidence="ECO:0000269|PubMed:23844911"
FT HELIX 10..28
FT /evidence="ECO:0007829|PDB:5ZUG"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:5ZUG"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:5ZUG"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:5ZUG"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:5ZUG"
FT HELIX 63..84
FT /evidence="ECO:0007829|PDB:5ZUG"
FT TURN 85..89
FT /evidence="ECO:0007829|PDB:5ZUG"
FT HELIX 96..115
FT /evidence="ECO:0007829|PDB:5ZUG"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5ZUG"
FT HELIX 122..144
FT /evidence="ECO:0007829|PDB:5ZUG"
FT HELIX 147..177
FT /evidence="ECO:0007829|PDB:5ZUG"
SQ SEQUENCE 188 AA; 20071 MW; 972101DD5949EBF4 CRC64;
MGNTKLANPA PLGLMGFGMT TILLNLHNVG YFALDGIILA MGIFYGGIAQ IFAGLLEYKK
GNTFGLTAFT SYGSFWLTLV AILLMPKLGL TDAPNAQFLG VYLGLWGVFT LFMFFGTLKG
ARVLQFVFFS LTVLFALLAI GNIAGNAAII HFAGWIGLIC GASAIYLAMG EVLNEQFGRT
VLPIGESH
