POTG_ECOLI
ID POTG_ECOLI Reviewed; 377 AA.
AC P31134;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Putrescine transport ATP-binding protein PotG {ECO:0000305};
DE EC=7.6.2.16 {ECO:0000269|PubMed:23719730};
GN Name=potG {ECO:0000303|PubMed:8416922}; OrderedLocusNames=b0855, JW5818;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, 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).
CC -!- FUNCTION: Part of the ABC transporter complex PotFGHI involved in
CC putrescine uptake (PubMed:8416922, PubMed:23719730). Responsible for
CC energy coupling to the transport system (PubMed:23719730). Imports
CC putrescine for maintenance of the optimal concentration of polyamines
CC necessary for cell growth in the presence of glucose (PubMed:23719730).
CC {ECO:0000269|PubMed:23719730, ECO:0000269|PubMed:8416922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + putrescine(out) = ADP + H(+) + phosphate +
CC putrescine(in); Xref=Rhea:RHEA:29995, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:326268, ChEBI:CHEBI:456216; EC=7.6.2.16;
CC Evidence={ECO:0000269|PubMed:23719730};
CC -!- ACTIVITY REGULATION: Transport is feedback inhibited by intracellular
CC polyamines. {ECO:0000269|PubMed:23719730}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.57 uM for putrescine {ECO:0000269|PubMed:23719730};
CC Vmax=23.0 nmol/min/mg enzyme {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: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24410.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M93239; AAA24410.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73942.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35566.2; -; Genomic_DNA.
DR PIR; B45313; B45313.
DR RefSeq; NP_415376.4; NC_000913.3.
DR RefSeq; WP_000996005.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P31134; -.
DR SMR; P31134; -.
DR BioGRID; 4263504; 531.
DR BioGRID; 849850; 3.
DR ComplexPortal; CPX-4384; Putrescine ABC transporter complex.
DR DIP; DIP-10532N; -.
DR IntAct; P31134; 4.
DR STRING; 511145.b0855; -.
DR TCDB; 3.A.1.11.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; P31134; -.
DR PRIDE; P31134; -.
DR EnsemblBacteria; AAC73942; AAC73942; b0855.
DR EnsemblBacteria; BAA35566; BAA35566; BAA35566.
DR GeneID; 945476; -.
DR KEGG; ecj:JW5818; -.
DR KEGG; eco:b0855; -.
DR PATRIC; fig|1411691.4.peg.1422; -.
DR EchoBASE; EB1587; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_6; -.
DR InParanoid; P31134; -.
DR OMA; RLHSGQM; -.
DR PhylomeDB; P31134; -.
DR BioCyc; EcoCyc:POTG-MON; -.
DR BioCyc; MetaCyc:POTG-MON; -.
DR PRO; PR:P31134; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; TAS:EcoCyc.
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:0015594; F:ABC-type putrescine transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015847; P:putrescine transport; IDA:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005893; Sp_pt_ABC_ATP-bd.
DR InterPro; IPR013611; Transp-assoc_OB_typ2.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08402; TOBE_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01187; potA; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..377
FT /note="Putrescine transport ATP-binding protein PotG"
FT /id="PRO_0000092760"
FT DOMAIN 20..250
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 52..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 377 AA; 41931 MW; 4C13E389C03CF76C CRC64;
MNDAIPRPQA KTRKALTPLL EIRNLTKSYD GQHAVDDVSL TIYKGEIFAL LGASGCGKST
LLRMLAGFEQ PSAGQIMLDG VDLSQVPPYL RPINMMFQSY ALFPHMTVEQ NIAFGLKQDK
LPKAEIASRV NEMLGLVHMQ EFAKRKPHQL SGGQRQRVAL ARSLAKRPKL LLLDEPMGAL
DKKLRDRMQL EVVDILERVG VTCVMVTHDQ EEAMTMAGRI AIMNRGKFVQ IGEPEEIYEH
PTTRYSAEFI GSVNVFEGVL KERQEDGLVL DSPGLVHPLK VDADASVVDN VPVHVALRPE
KIMLCEEPPA NGCNFAVGEV IHIAYLGDLS VYHVRLKSGQ MISAQLQNAH RHRKGLPTWG
DEVRLCWEVD SCVVLTV
