ID   POTA_LEGPA              Reviewed;         364 AA.
AC   Q5X627;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
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}; OrderedLocusNames=lpp1143;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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   -!- 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   -!- 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}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01726}.
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; CR628336; CAH12294.1; -; Genomic_DNA.
DR   RefSeq; WP_011213497.1; NC_006368.1.
DR   AlphaFoldDB; Q5X627; -.
DR   SMR; Q5X627; -.
DR   KEGG; lpp:lpp1143; -.
DR   LegioList; lpp1143; -.
DR   HOGENOM; CLU_000604_1_1_6; -.
DR   OMA; IHVMRFN; -.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0015417; F:ABC-type polyamine transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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.
DR   PROSITE; PS51305; POTA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..364
FT                   /note="Spermidine/putrescine import ATP-binding protein
FT                   PotA"
FT                   /id="PRO_0000286240"
FT   DOMAIN          6..236
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
SQ   SEQUENCE   364 AA;  41398 MW;  DF2CDF38EA14BAFE CRC64;
     MTTPLIEIRQ IYKSYGNTPI LNNVSLNVNH GEFLTLLGPS GCGKTTLLRL ISGFEQPTQG
     EIFINGQCVN QLPPQKRDVH TVFQSYALFP HLSVFENVAF ALRCKKTSNQ EIKERVFDAL
     KLVQLELLAE RNVKQLSGGQ QQRVAIARAI INRPQVLLLD EPLSSLDYRL RKAMQSELKQ
     LQKTLNMTFI FVTHDQEEAL SMSDRIVVFN HGHIEQIGTP KAVYETPANL HVAMFIGEAN
     IFDIQVHTVK DQDIVTNIEG IQLSCKNTGN YQVNEWLHLI VRPEDIRVWS LSEVEKTEGM
     LPGRIVDIIY KGSTVDLKVE LSSGKIINAS EFFDEDDDKL EYTLHETVWV QWLPGWEVLL
     PYEG