ID   POTA_AGGAC              Reviewed;         372 AA.
AC   O85818;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
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};
OS   Aggregatibacter actinomycetemcomitans (Actinobacillus
OS   actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43718 / FDC Y4 / Serotype b;
RA   Winston J.L., Sezate S.A., Dyer D.W., McLaughlin R.E.;
RT   "Demonstration of a polyamine requirement for growth of Actinobacillus
RT   actinomycetemcomitans, and identification of the putative polyamine
RT   transport operon.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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; AF077856; AAC27495.1; -; Genomic_DNA.
DR   AlphaFoldDB; O85818; -.
DR   SMR; O85818; -.
DR   STRING; 714.ACT75_09915; -.
DR   eggNOG; COG3842; Bacteria.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0015594; F:ABC-type putrescine transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..372
FT                   /note="Spermidine/putrescine import ATP-binding protein
FT                   PotA"
FT                   /id="PRO_0000286187"
FT   DOMAIN          11..241
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
SQ   SEQUENCE   372 AA;  42276 MW;  338F84A481B9D853 CRC64;
     MENTVQNKPI IELRSITKSY GSNTIIKDFN LTINNGEFLT ILGPSGCGKT TVLRLLAGLE
     ELDSGNIILD GEDITNVPAE KRHVNTVFQS YALFPHMTIF ENVAFGLRMQ KVPEAEIKPR
     VLEALRMVQL EEMADRKPTQ LSGGQQQRIA IARAVVNKPK VLLLDESLSA LDYKLRKQMQ
     YELKVLQRQL GITFIFVTHD QEEAITMSDR IVLLRKGKIA QDGSPREIYE EPANLFVARF
     IGEINVFDAT VIERKSENVV LANVEGRVCD IYTDIPVKKD QQLQVLLRPE DIVIKELDEH
     EHSKAIIGHI IDRTYKGMTL ESTVEFEQNG KRGLVSEFFN EDDPHMDHSI GQRVGITWHE
     GWEVVLNDED NQ