POTA_ECOLI
ID POTA_ECOLI Reviewed; 378 AA.
AC P69874; P23858;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Spermidine/putrescine import ATP-binding protein PotA {ECO:0000255|HAMAP-Rule:MF_01726};
DE EC=7.6.2.11 {ECO:0000255|HAMAP-Rule:MF_01726};
GN Name=potA {ECO:0000255|HAMAP-Rule:MF_01726};
GN OrderedLocusNames=b1126, JW1112;
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 IN SPERMIDINE AND PUTRESCINE
RP TRANSPORT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=1939142; DOI=10.1016/s0021-9258(18)54799-2;
RA Furuchi T., Kashiwagi K., Kobayashi H., Igarashi K.;
RT "Characteristics of the gene for a spermidine and putrescine transport
RT system that maps at 15 min on the Escherichia coli chromosome.";
RL J. Biol. Chem. 266:20928-20933(1991).
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 27-30 AND 360-378, BIOPHYSICOCHEMICAL PROPERTIES,
RP ATPASE ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF CYS-26; CYS-54 AND CYS-276.
RC STRAIN=K12;
RX PubMed=7592703; DOI=10.1074/jbc.270.43.25377;
RA Kashiwagi K., Endo H., Kobayashi H., Takio K., Igarashi K.;
RT "Spermidine-preferential uptake system in Escherichia coli. ATP hydrolysis
RT by PotA protein and its association with membranes.";
RL J. Biol. Chem. 270:25377-25382(1995).
RN [6]
RP FUNCTION IN SPERMIDINE AND PUTRESCINE TRANSPORT, ATPASE ACTIVITY, AND
RP ACTIVITY REGULATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2249996; DOI=10.1016/s0021-9258(17)45300-2;
RA Kashiwagi K., Hosokawa N., Furuchi T., Kobayashi H., Sasakawa C.,
RA Yoshikawa M., Igarashi K.;
RT "Isolation of polyamine transport-deficient mutants of Escherichia coli and
RT cloning of the genes for polyamine transport proteins.";
RL J. Biol. Chem. 265:20893-20897(1990).
RN [7]
RP FUNCTION IN SPERMIDINE TRANSPORT, ATPASE ACTIVITY, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF VAL-135.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8366082; DOI=10.1016/s0021-9258(19)36522-6;
RA Kashiwagi K., Miyamoto S., Nukui E., Kobayashi H., Igarashi K.;
RT "Functions of potA and potD proteins in spermidine-preferential uptake
RT system in Escherichia coli.";
RL J. Biol. Chem. 268:19358-19363(1993).
RN [8]
RP TRANSCRIPTIONAL REGULATION BY POTD.
RC STRAIN=K12;
RX PubMed=9890949; DOI=10.1074/jbc.274.4.1942;
RA Antognoni F., Del Duca S., Kuraishi A., Kawabe E., Fukuchi-Shimogori T.,
RA Kashiwagi K., Igarashi K.;
RT "Transcriptional inhibition of the operon for the spermidine uptake system
RT by the substrate-binding protein PotD.";
RL J. Biol. Chem. 274:1942-1948(1999).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, ATPASE ACTIVITY, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF PHE-27; PHE-45; LEU-60; LEU-76; VAL-135; ASP-172 AND
RP GLU-297.
RC STRAIN=K12;
RX PubMed=11976340; DOI=10.1074/jbc.m202849200;
RA Kashiwagi K., Innami A., Zenda R., Tomitori H., Igarashi K.;
RT "The ATPase activity and the functional domain of PotA, a component of the
RT spermidine-preferential uptake system in Escherichia coli.";
RL J. Biol. Chem. 277:24212-24219(2002).
CC -!- FUNCTION: Part of the ABC transporter complex PotABCD involved in
CC spermidine/putrescine import. Responsible for energy coupling to the
CC transport system. {ECO:0000255|HAMAP-Rule:MF_01726,
CC ECO:0000269|PubMed:1939142, ECO:0000269|PubMed:2249996,
CC ECO:0000269|PubMed:8366082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP
CC + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.;
CC EC=7.6.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01726};
CC -!- ACTIVITY REGULATION: Strongly inhibited by carbonyl cyanide m-
CC chlorophenylhydrazone (CCCP), and by spermidine via its interaction
CC with the C-terminus. Also inhibited by N-ethylmaleimide and p-
CC chloromercuribenzoic acid. Partially inhibited by KCN.
CC {ECO:0000269|PubMed:11976340, ECO:0000269|PubMed:2249996,
CC ECO:0000269|PubMed:7592703, ECO:0000269|PubMed:8366082}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=385 uM for ATP {ECO:0000269|PubMed:11976340,
CC ECO:0000269|PubMed:7592703};
CC Vmax=400 nmol/min/mg enzyme {ECO:0000269|PubMed:11976340,
CC ECO:0000269|PubMed:7592703};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PotA),
CC two transmembrane proteins (PotB and PotC) and a solute-binding protein
CC (PotD). {ECO:0000255|HAMAP-Rule:MF_01726}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01726, ECO:0000269|PubMed:1939142, ECO:0000269|PubMed:7592703};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01726,
CC ECO:0000269|PubMed:1939142, ECO:0000269|PubMed:7592703}.
CC -!- INDUCTION: Transcription is inhibited by PotD precursor, probably only
CC when excess amounts of PotD are produced. {ECO:0000269|PubMed:9890949}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC Spermidine/putrescine importer (TC 3.A.1.11.1) family.
CC {ECO:0000255|HAMAP-Rule:MF_01726}.
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DR EMBL; M64519; AAC37038.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74210.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35946.1; -; Genomic_DNA.
DR PIR; A40840; A40840.
DR RefSeq; NP_415644.1; NC_000913.3.
DR RefSeq; WP_000531594.1; NZ_SSZK01000010.1.
DR AlphaFoldDB; P69874; -.
DR SMR; P69874; -.
DR BioGRID; 4261674; 16.
DR BioGRID; 850680; 1.
DR ComplexPortal; CPX-4383; Spermidine ABC transporter complex.
DR IntAct; P69874; 2.
DR STRING; 511145.b1126; -.
DR TCDB; 3.A.1.11.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P69874; -.
DR PaxDb; P69874; -.
DR PRIDE; P69874; -.
DR EnsemblBacteria; AAC74210; AAC74210; b1126.
DR EnsemblBacteria; BAA35946; BAA35946; BAA35946.
DR GeneID; 66670607; -.
DR GeneID; 946323; -.
DR KEGG; ecj:JW1112; -.
DR KEGG; eco:b1126; -.
DR PATRIC; fig|1411691.4.peg.1141; -.
DR EchoBASE; EB0742; -.
DR eggNOG; COG3842; Bacteria.
DR InParanoid; P69874; -.
DR OMA; IHVMRFN; -.
DR PhylomeDB; P69874; -.
DR BioCyc; EcoCyc:POTA-MON; -.
DR BioCyc; MetaCyc:POTA-MON; -.
DR PRO; PR:P69874; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; TAS:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015417; F:ABC-type polyamine transporter activity; IDA:EcoCyc.
DR GO; GO:0015594; F:ABC-type putrescine transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0000166; F:nucleotide binding; IDA:EcoCyc.
DR GO; GO:0015847; P:putrescine transport; IDA:EcoCyc.
DR GO; GO:1903711; P:spermidine transmembrane transport; IDA:EcoCyc.
DR CDD; cd03300; ABC_PotA_N; 1.
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; IPR017879; PotA_ATP-bd.
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.
DR PROSITE; PS51305; POTA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Membrane; Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..378
FT /note="Spermidine/putrescine import ATP-binding protein
FT PotA"
FT /id="PRO_0000092746"
FT DOMAIN 18..248
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT MUTAGEN 26
FT /note="C->A: Lower ATPase activity and transport
FT efficiency."
FT /evidence="ECO:0000269|PubMed:7592703"
FT MUTAGEN 27
FT /note="F->L: Lower ATPase activity and transport
FT efficiency."
FT /evidence="ECO:0000269|PubMed:11976340"
FT MUTAGEN 45
FT /note="F->L: Lower ATPase activity and transport
FT efficiency."
FT /evidence="ECO:0000269|PubMed:11976340"
FT MUTAGEN 54
FT /note="C->T: Loss of ATPase activity and transport."
FT /evidence="ECO:0000269|PubMed:7592703"
FT MUTAGEN 60
FT /note="L->F: Lower ATPase activity and transport
FT efficiency."
FT /evidence="ECO:0000269|PubMed:11976340"
FT MUTAGEN 76
FT /note="L->P: Lower ATPase activity and transport
FT efficiency."
FT /evidence="ECO:0000269|PubMed:11976340"
FT MUTAGEN 135
FT /note="V->M: Loss of ATPase activity and transport."
FT /evidence="ECO:0000269|PubMed:11976340,
FT ECO:0000269|PubMed:8366082"
FT MUTAGEN 172
FT /note="D->N: Loss of ATPase activity and transport."
FT /evidence="ECO:0000269|PubMed:11976340"
FT MUTAGEN 276
FT /note="C->A: Lower ATPase activity and transport
FT efficiency."
FT /evidence="ECO:0000269|PubMed:7592703"
FT MUTAGEN 297
FT /note="E->K,D: Lower ATPase activity and transport
FT efficiency."
FT /evidence="ECO:0000269|PubMed:11976340"
FT MUTAGEN 297
FT /note="E->Q: Loss of ATPase activity and transport."
FT /evidence="ECO:0000269|PubMed:11976340"
SQ SEQUENCE 378 AA; 43028 MW; 14DCA99329A344F3 CRC64;
MGQSKKLNKQ PSSLSPLVQL AGIRKCFDGK EVIPQLDLTI NNGEFLTLLG PSGCGKTTVL
RLIAGLETVD SGRIMLDNED ITHVPAENRY VNTVFQSYAL FPHMTVFENV AFGLRMQKTP
AAEITPRVME ALRMVQLETF AQRKPHQLSG GQQQRVAIAR AVVNKPRLLL LDESLSALDY
KLRKQMQNEL KALQRKLGIT FVFVTHDQEE ALTMSDRIVV MRDGRIEQDG TPREIYEEPK
NLFVAGFIGE INMFNATVIE RLDEQRVRAN VEGRECNIYV NFAVEPGQKL HVLLRPEDLR
VEEINDDNHA EGLIGYVRER NYKGMTLESV VELENGKMVM VSEFFNEDDP DFDHSLDQKM
AINWVESWEV VLADEEHK
