GHXP_ECOLI
ID GHXP_ECOLI Reviewed; 449 AA.
AC P0AF52; P32702; Q2M6P0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Guanine/hypoxanthine permease GhxP;
GN Name=ghxP; Synonyms=yjcD; OrderedLocusNames=b4064, JW4025;
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 SUBCELLULAR LOCATION [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).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY,
RP GENE NAME, AND MUTAGENESIS OF THR-35; ALA-88; ASP-271; THR-275; ASP-302;
RP ILE-321; GLU-322 AND SER-323.
RC STRAIN=K12;
RX PubMed=24214977; DOI=10.1074/jbc.m113.523340;
RA Papakostas K., Botou M., Frillingos S.;
RT "Functional identification of the hypoxanthine/guanine transporters YjcD
RT and YgfQ and the adenine transporters PurP and YicO of Escherichia coli K-
RT 12.";
RL J. Biol. Chem. 288:36827-36840(2013).
CC -!- FUNCTION: High-affinity transporter for guanine and hypoxanthine.
CC {ECO:0000269|PubMed:24214977}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 uM for guanine {ECO:0000269|PubMed:24214977};
CC KM=11.2 uM for hypoxanthine {ECO:0000269|PubMed:24214977};
CC Vmax=4.0 nmol/min/mg enzyme with guanine as substrate
CC {ECO:0000269|PubMed:24214977};
CC Vmax=2.7 nmol/min/mg enzyme with hypoxanthine as substrate
CC {ECO:0000269|PubMed:24214977};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:24214977}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:24214977}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. Azg-like subfamily. {ECO:0000305}.
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DR EMBL; U00006; AAC43158.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77034.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78066.1; -; Genomic_DNA.
DR PIR; G65214; G65214.
DR RefSeq; NP_418488.1; NC_000913.3.
DR RefSeq; WP_000106882.1; NZ_STEB01000014.1.
DR AlphaFoldDB; P0AF52; -.
DR BioGRID; 4262672; 293.
DR DIP; DIP-48113N; -.
DR IntAct; P0AF52; 1.
DR STRING; 511145.b4064; -.
DR TCDB; 2.A.40.7.5; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR jPOST; P0AF52; -.
DR PaxDb; P0AF52; -.
DR PRIDE; P0AF52; -.
DR EnsemblBacteria; AAC77034; AAC77034; b4064.
DR EnsemblBacteria; BAE78066; BAE78066; BAE78066.
DR GeneID; 66672020; -.
DR GeneID; 948565; -.
DR KEGG; ecj:JW4025; -.
DR KEGG; eco:b4064; -.
DR PATRIC; fig|1411691.4.peg.2640; -.
DR EchoBASE; EB1883; -.
DR eggNOG; COG2252; Bacteria.
DR HOGENOM; CLU_024508_0_1_6; -.
DR InParanoid; P0AF52; -.
DR OMA; WVLTNLP; -.
DR PhylomeDB; P0AF52; -.
DR BioCyc; EcoCyc:EG11939-MON; -.
DR BioCyc; MetaCyc:EG11939-MON; -.
DR SABIO-RK; P0AF52; -.
DR PRO; PR:P0AF52; -.
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:0015208; F:guanine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0098710; P:guanine import across plasma membrane; IMP:EcoCyc.
DR GO; GO:0035344; P:hypoxanthine transport; IMP:EcoCyc.
DR InterPro; IPR045018; Azg-like.
DR InterPro; IPR006043; NCS2.
DR PANTHER; PTHR43337; PTHR43337; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..449
FT /note="Guanine/hypoxanthine permease GhxP"
FT /id="PRO_0000169720"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..59
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..97
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..109
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..180
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..254
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..314
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..330
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..360
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 386..421
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 35
FT /note="T->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 35
FT /note="T->H: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 88
FT /note="A->G,S: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 271
FT /note="D->A,N: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 271
FT /note="D->E: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 275
FT /note="T->A,D,N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 275
FT /note="T->S: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 302
FT /note="D->E: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 302
FT /note="D->N: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 321
FT /note="I->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 321
FT /note="I->E: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 322
FT /note="E->D: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 322
FT /note="E->Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
FT MUTAGEN 323
FT /note="S->A,N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24214977"
SQ SEQUENCE 449 AA; 45711 MW; BDBFE2F057E45910 CRC64;
MSTPSARTGG SLDAWFKISQ RGSTVRQEVV AGLTTFLAMV YSVIVVPGML GKAGFPPAAV
FVATCLVAGL GSIVMGLWAN LPLAIGCAIS LTAFTAFSLV LGQHISVPVA LGAVFLMGVL
FTVISATGIR SWILRNLPHG VAHGTGIGIG LFLLLIAANG VGLVIKNPLD GLPVALGDFA
TFPVIMSLVG LAVIIGLEKL KVPGGILLTI IGISIVGLIF DPNVHFSGVF AMPSLSDENG
NSLIGSLDIM GALNPVVLPS VLALVMTAVF DATGTIRAVA GQANLLDKDG QIIDGGKALT
TDSMSSVFSG LVGAAPAAVY IESAAGTAAG GKTGLTAITV GVLFLLILFL SPLSYLVPGY
ATAPALMYVG LLMLSNVAKI DFADFVDAMA GLVTAVFIVL TCNIVTGIMI GFATLVIGRL
VSGEWRKLNI GTVVIAVALV TFYAGGWAI
