POTF_ECOLI
ID POTF_ECOLI Reviewed; 370 AA.
AC P31133; P77289;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Putrescine-binding periplasmic protein PotF;
DE Flags: Precursor;
GN Name=potF {ECO:0000303|PubMed:8416922}; OrderedLocusNames=b0854, JW0838;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-46, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=8416922; DOI=10.1016/s0021-9258(18)54126-0;
RA Pistocchi R., Kashiwagi K., Miyamoto S., Nukui E., Sadakata Y.,
RA Kobayashi H., Igarashi K.;
RT "Characteristics of the operon for a putrescine transport system that maps
RT at 19 minutes on the Escherichia coli chromosome.";
RL J. Biol. Chem. 268:146-152(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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].
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 PROTEIN SEQUENCE OF 27-36.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=23719730; DOI=10.1007/s00726-013-1517-x;
RA Terui Y., Saroj S.D., Sakamoto A., Yoshida T., Higashi K., Kurihara S.,
RA Suzuki H., Toida T., Kashiwagi K., Igarashi K.;
RT "Properties of putrescine uptake by PotFGHI and PuuP and their
RT physiological significance in Escherichia coli.";
RL Amino Acids 46:661-670(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9761835; DOI=10.1107/s0907444997009049;
RA Vassylyev D.G., Kashiwagi T., Tomitori H., Kashiwagi K., Igarashi K.,
RA Morikawa K.;
RT "Crystallization and preliminary X-ray analysis of the periplasmic receptor
RT (PotF) of the putrescine transport system in Escherichia coli.";
RL Acta Crystallogr. D 54:132-134(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH PUTRESCINE, AND
RP DISULFIDE BOND.
RX PubMed=9651355; DOI=10.1074/jbc.273.28.17604;
RA Vassylyev D.G., Tomitori H., Kashiwagi K., Morikawa K., Igarashi K.;
RT "Crystal structure and mutational analysis of the Escherichia coli
RT putrescine receptor. Structural basis for substrate specificity.";
RL J. Biol. Chem. 273:17604-17609(1998).
CC -!- FUNCTION: Part of the ABC transporter complex PotFGHI involved in
CC putrescine uptake (PubMed:8416922, PubMed:23719730). Binds putrescine
CC (PubMed:8416922, PubMed:9651355). Imports putrescine for maintenance of
CC the optimal concentration of polyamines necessary for cell growth in
CC the presence of glucose (PubMed:23719730).
CC {ECO:0000269|PubMed:23719730, ECO:0000269|PubMed:8416922,
CC ECO:0000269|PubMed:9651355}.
CC -!- ACTIVITY REGULATION: Transport is feedback inhibited by intracellular
CC polyamines. {ECO:0000269|PubMed:23719730}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PotG),
CC two transmembrane proteins (PotH and PotI) and a solute-binding protein
CC (PotF). {ECO:0000269|PubMed:23719730, ECO:0000269|PubMed:8416922}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8416922}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein PotD/PotF
CC family. {ECO:0000305}.
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DR EMBL; M93239; AAA24409.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73941.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35565.1; -; Genomic_DNA.
DR PIR; F64823; F64823.
DR RefSeq; NP_415375.1; NC_000913.3.
DR RefSeq; WP_000126072.1; NZ_SSZK01000002.1.
DR PDB; 1A99; X-ray; 2.20 A; A/B/C/D=27-370.
DR PDB; 4JDF; X-ray; 1.69 A; A=27-370.
DR PDB; 6YE0; X-ray; 1.63 A; A/B=27-370.
DR PDB; 6YE6; X-ray; 1.56 A; A/B=27-370.
DR PDB; 6YE7; X-ray; 1.60 A; A/B=27-370.
DR PDB; 6YE8; X-ray; 1.50 A; A/B=27-370.
DR PDB; 6YEB; X-ray; 1.97 A; A/B=27-370.
DR PDB; 6YEC; X-ray; 2.09 A; A/B=27-370.
DR PDB; 6YED; X-ray; 2.18 A; A/B=27-370.
DR PDB; 7OYT; X-ray; 1.60 A; A=27-370.
DR PDB; 7OYU; X-ray; 1.95 A; A=27-370.
DR PDB; 7OYX; X-ray; 1.37 A; A/B=27-370.
DR PDB; 7OYY; X-ray; 1.36 A; A=27-370.
DR PDB; 7OYZ; X-ray; 1.49 A; A=27-370.
DR PDBsum; 1A99; -.
DR PDBsum; 4JDF; -.
DR PDBsum; 6YE0; -.
DR PDBsum; 6YE6; -.
DR PDBsum; 6YE7; -.
DR PDBsum; 6YE8; -.
DR PDBsum; 6YEB; -.
DR PDBsum; 6YEC; -.
DR PDBsum; 6YED; -.
DR PDBsum; 7OYT; -.
DR PDBsum; 7OYU; -.
DR PDBsum; 7OYX; -.
DR PDBsum; 7OYY; -.
DR PDBsum; 7OYZ; -.
DR AlphaFoldDB; P31133; -.
DR SMR; P31133; -.
DR BioGRID; 4259994; 13.
DR ComplexPortal; CPX-4384; Putrescine ABC transporter complex.
DR DIP; DIP-10531N; -.
DR IntAct; P31133; 2.
DR STRING; 511145.b0854; -.
DR DrugBank; DB01917; Putrescine.
DR TCDB; 3.A.1.11.2; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P31133; -.
DR PaxDb; P31133; -.
DR PRIDE; P31133; -.
DR EnsemblBacteria; AAC73941; AAC73941; b0854.
DR EnsemblBacteria; BAA35565; BAA35565; BAA35565.
DR GeneID; 66670872; -.
DR GeneID; 945480; -.
DR KEGG; ecj:JW0838; -.
DR KEGG; eco:b0854; -.
DR PATRIC; fig|1411691.4.peg.1423; -.
DR EchoBASE; EB1586; -.
DR eggNOG; COG0687; Bacteria.
DR HOGENOM; CLU_026974_1_4_6; -.
DR InParanoid; P31133; -.
DR OMA; SNWTEYM; -.
DR PhylomeDB; P31133; -.
DR BioCyc; EcoCyc:POTF-MON; -.
DR BioCyc; MetaCyc:POTF-MON; -.
DR EvolutionaryTrace; P31133; -.
DR PRO; PR:P31133; -.
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:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0019810; F:putrescine binding; IDA:EcoCyc.
DR GO; GO:0015847; P:putrescine transport; IDA:EcoCyc.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR001188; Sperm_putr-bd.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PIRSF; PIRSF019574; Periplasmic_polyamine_BP; 1.
DR PRINTS; PR00909; SPERMDNBNDNG.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:8416922,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 27..370
FT /note="Putrescine-binding periplasmic protein PotF"
FT /id="PRO_0000031842"
FT BINDING 38
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000269|PubMed:9651355"
FT BINDING 247
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000269|PubMed:9651355"
FT BINDING 278
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000269|PubMed:9651355"
FT DISULFID 175..239
FT /evidence="ECO:0000269|PubMed:9651355"
FT CONFLICT 29
FT /note="Q -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..217
FT /note="KL -> NV (in Ref. 1; AAA24409)"
FT /evidence="ECO:0000305"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:7OYY"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:7OYY"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:7OYY"
FT TURN 92..96
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:7OYY"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:7OYY"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:7OYY"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:7OYY"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:7OYY"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:7OYY"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:7OYY"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:7OYY"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:7OYY"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:7OYY"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:7OYY"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:7OYY"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:7OYT"
FT HELIX 353..368
FT /evidence="ECO:0007829|PDB:7OYY"
SQ SEQUENCE 370 AA; 40840 MW; E7AA745A35BFDAD1 CRC64;
MTALNKKWLS GLVAGALMAV SVGTLAAEQK TLHIYNWSDY IAPDTVANFE KETGIKVVYD
VFDSNEVLEG KLMAGSTGFD LVVPSASFLE RQLTAGVFQP LDKSKLPEWK NLDPELLKLV
AKHDPDNKFA MPYMWATTGI GYNVDKVKAV LGENAPVDSW DLILKPENLE KLKSCGVSFL
DAPEEVFATV LNYLGKDPNS TKADDYTGPA TDLLLKLRPN IRYFHSSQYI NDLANGDICV
AIGWAGDVWQ ASNRAKEAKN GVNVSFSIPK EGAMAFFDVF AMPADAKNKD EAYQFLNYLL
RPDVVAHISD HVFYANANKA ATPLVSAEVR ENPGIYPPAD VRAKLFTLKV QDPKIDRVRT
RAWTKVKSGK
