SAPD_ECOLI
ID SAPD_ECOLI Reviewed; 330 AA.
AC P0AAH4; P36635;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putrescine export system ATP-binding protein SapD {ECO:0000303|PubMed:27803167};
GN Name=sapD; Synonyms=trkE {ECO:0000303|PubMed:11700350};
GN OrderedLocusNames=b1291, JW1284;
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 MUTAGENESIS OF LYS-46;
RP GLY-162; GLN-165 AND ASP-183.
RC STRAIN=K12 / FRAG5;
RX PubMed=11700350; DOI=10.1099/00221287-147-11-2991;
RA Harms C., Domoto Y., Celik C., Rahe E., Stumpe S., Schmid R., Nakamura T.,
RA Bakker E.P.;
RT "Identification of the ABC protein SapD as the subunit that confers ATP
RT dependence to the K+-uptake systems Trk(H) and Trk(G) from Escherichia coli
RT K-12.";
RL Microbiology 147:2991-3003(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-330.
RA Bergler H., Ebeling A., Fuchsbichler S., Hogenauer G., Turnowsky F.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION IN PUTRESCINE EXPORT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=27803167; DOI=10.1074/jbc.m116.762450;
RA Sugiyama Y., Nakamura A., Matsumoto M., Kanbe A., Sakanaka M., Higashi K.,
RA Igarashi K., Katayama T., Suzuki H., Kurihara S.;
RT "A novel putrescine exporter SapBCDF of Escherichia coli.";
RL J. Biol. Chem. 291:26343-26351(2016).
CC -!- FUNCTION: Part of a putrescine export transport system, does not play a
CC role in resistance to antimicrobial peptides (PubMed:27803167).
CC Stimulates K(+)-uptake proteins TrkG and TrkH to import K(+), may act
CC via ATP-binding rather than ATP hydrolysis (PubMed:11700350).
CC {ECO:0000269|PubMed:11700350, ECO:0000269|PubMed:27803167}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Single mutation, decreased extracellular
CC putrescine, in an sapBCDF operon deletion no change in resistance to
CC antimicrobial peptide LL-37. {ECO:0000269|PubMed:27803167}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; X97282; CAA65940.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74373.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14844.1; -; Genomic_DNA.
DR EMBL; U08190; AAA17670.1; -; Unassigned_DNA.
DR PIR; F64877; F64877.
DR RefSeq; NP_415807.1; NC_000913.3.
DR RefSeq; WP_001128858.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P0AAH4; -.
DR SMR; P0AAH4; -.
DR BioGRID; 4260128; 352.
DR ComplexPortal; CPX-4422; Putative peptide ABC transporter.
DR DIP; DIP-10825N; -.
DR IntAct; P0AAH4; 5.
DR STRING; 511145.b1291; -.
DR TCDB; 3.A.1.5.42; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AAH4; -.
DR PaxDb; P0AAH4; -.
DR PRIDE; P0AAH4; -.
DR EnsemblBacteria; AAC74373; AAC74373; b1291.
DR EnsemblBacteria; BAA14844; BAA14844; BAA14844.
DR GeneID; 67417384; -.
DR GeneID; 946203; -.
DR KEGG; ecj:JW1284; -.
DR KEGG; eco:b1291; -.
DR PATRIC; fig|1411691.4.peg.988; -.
DR EchoBASE; EB2210; -.
DR eggNOG; COG4172; Bacteria.
DR HOGENOM; CLU_000604_1_23_6; -.
DR InParanoid; P0AAH4; -.
DR OMA; PHGRVKA; -.
DR PhylomeDB; P0AAH4; -.
DR BioCyc; EcoCyc:SAPD-MON; -.
DR BioCyc; MetaCyc:SAPD-MON; -.
DR BRENDA; 7.6.2.11; 2026.
DR PRO; PR:P0AAH4; -.
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:0005524; F:ATP binding; IMP:EcoCyc.
DR GO; GO:0015489; F:putrescine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015833; P:peptide transport; IC:ComplexPortal.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:EcoCyc.
DR GO; GO:0015847; P:putrescine transport; IMP:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR013563; Oligopep_ABC_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08352; oligo_HPY; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Nucleotide-binding; Potassium; Potassium transport; Reference proteome;
KW Transport.
FT CHAIN 1..330
FT /note="Putrescine export system ATP-binding protein SapD"
FT /id="PRO_0000092962"
FT DOMAIN 6..259
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 46
FT /note="K->G,I,Q,R: 25% to 50% stimulation of K(+) uptake by
FT TrkH."
FT /evidence="ECO:0000269|PubMed:11700350"
FT MUTAGEN 46
FT /note="Missing: Almost no stimulation of K(+) uptake by
FT TrkH."
FT /evidence="ECO:0000269|PubMed:11700350"
FT MUTAGEN 162
FT /note="G->A: 80% stimulation of K(+) uptake by TrkH."
FT /evidence="ECO:0000269|PubMed:11700350"
FT MUTAGEN 165
FT /note="Q->L: 60% stimulation of K(+) uptake by TrkH."
FT /evidence="ECO:0000269|PubMed:11700350"
FT MUTAGEN 183
FT /note="D->E: About 60% stimulation of K(+) uptake by TrkH."
FT /evidence="ECO:0000269|PubMed:11700350"
FT MUTAGEN 183
FT /note="D->K,N: 15% to 20% stimulation of K(+) uptake by
FT TrkH."
FT /evidence="ECO:0000269|PubMed:11700350"
SQ SEQUENCE 330 AA; 37661 MW; 1326280E475628E0 CRC64;
MPLLDIRNLT IEFKTGDEWV KAVDRVSMTL TEGEIRGLVG ESGSGKSLIA KAICGVNKDN
WRVTADRMRF DDIDLLRLSA RERRKLVGHN VSMIFQEPQS CLDPSERVGR QLMQNIPAWT
YKGRWWQRFG WRKRRAIELL HRVGIKDHKD AMRSFPYELT EGECQKVMIA IALANQPRLL
IADEPTNSME PTTQAQIFRL LTRLNQNSNT TILLISHDLQ MLSQWADKIN VLYCGQTVET
APSKELVTMP HHPYTQALIR AIPDFGSAMP HKSRLNTLPG AIPLLEQLPI GCRLGPRCPY
AQRECIVTPR LTGAKNHLYA CHFPLNMEKE
