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Database: UniProt
Entry: A0A1H8PF43_9BURK
LinkDB: A0A1H8PF43_9BURK
Original site: A0A1H8PF43_9BURK 
ID   A0A1H8PF43_9BURK        Unreviewed;       375 AA.
AC   A0A1H8PF43;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Spermidine/putrescine import ATP-binding protein PotA {ECO:0000256|RuleBase:RU364083};
DE            EC=7.6.2.11 {ECO:0000256|RuleBase:RU364083};
GN   Name=potA {ECO:0000256|RuleBase:RU364083};
GN   ORFNames=SAMN05428959_107213 {ECO:0000313|EMBL:SEO40173.1};
OS   Duganella sp. CF517.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEO40173.1, ECO:0000313|Proteomes:UP000198691};
RN   [1] {ECO:0000313|Proteomes:UP000198691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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:0000256|RuleBase:RU364083}.
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:0000256|RuleBase:RU364083};
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:0000256|RuleBase:RU364083}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Spermidine/putrescine importer (TC 3.A.1.11.1) family.
CC       {ECO:0000256|RuleBase:RU364083}.
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DR   EMBL; FODC01000007; SEO40173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8PF43; -.
DR   STRING; 1881038.SAMN05428959_107213; -.
DR   OrthoDB; 5298774at2; -.
DR   Proteomes; UP000198691; Unassembled WGS sequence.
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   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; PotA-like.
DR   InterPro; IPR013611; Transp-assoc_OB_typ2.
DR   NCBIfam; TIGR01187; potA; 1.
DR   PANTHER; PTHR42781:SF5; PUTRESCINE TRANSPORT ATP-BINDING PROTEIN POTG; 1.
DR   PANTHER; PTHR42781; SPERMIDINE/PUTRESCINE IMPORT ATP-BINDING PROTEIN POTA; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08402; TOBE_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; MOP-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364083};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU364083};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364083};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364083};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198691};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU364083};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364083}.
FT   DOMAIN          11..241
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   375 AA;  41210 MW;  433C6C34A1E9129E CRC64;
     MTIERAAEPF LLIRNLVKEF DGVRAVNDVS VAINKGEIFA LLGSSGCGKS TLLRMLAGFE
     TPTQGQITLA GKDIVSVPPY QRPINMMFQS YALFPHLSVW DNIAFGLRRD GLPKDEISAR
     VEQMLNLVQL AAYGKRKPHQ LSGGQQQRVA LARSLAKRPQ LLLLDEPLGA LDKKLRERTQ
     MELVGIIEEV GVTCVMVTHD QDEAMSMATR IAVMSEGRIL QVGPPGEIYE TPNCRFVADF
     IGSVNLFNGS VAVDEPDHVI IDTPEGRHYV THGITGTMGM PVSVAVRPEK IALQTEAPTL
     EQRANAGEHG YNCVQGAITA MAYFGNETLY HVRLDSGMEI KVSRTNAARH DDAALKRDQR
     VYAWWDGADV VVLTS
//
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