ID A0A1Y0N4S2_9BURK Unreviewed; 366 AA.
AC A0A1Y0N4S2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
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_1 {ECO:0000313|EMBL:ARV17672.1};
GN Synonyms=potA {ECO:0000256|RuleBase:RU364083};
GN ORFNames=AEP_00713 {ECO:0000313|EMBL:ARV17672.1};
OS Curvibacter sp. AEP1-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Curvibacter.
OX NCBI_TaxID=1844971 {ECO:0000313|EMBL:ARV17672.1, ECO:0000313|Proteomes:UP000196261};
RN [1] {ECO:0000313|EMBL:ARV17672.1, ECO:0000313|Proteomes:UP000196261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AEP1-3 {ECO:0000313|EMBL:ARV17672.1,
RC ECO:0000313|Proteomes:UP000196261};
RA Foret S., Pietschke C., Fraune S.;
RT "Curvibacter sp. AEP1.3.";
RL Submitted (MAY-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; CP015698; ARV17672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0N4S2; -.
DR OrthoDB; 5298774at2; -.
DR Proteomes; UP000196261; Chromosome.
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}; Hydrolase {ECO:0000313|EMBL:ARV17672.1};
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:UP000196261};
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 366 AA; 40357 MW; 7CC78D5571B9B739 CRC64;
MAVQPDKMGY LVTEKLVKRF DEAVAVDEVS LSIGQGEIFA LLGSSGCGKS TLLRMLAGFE
SPTSGRILLG GQDVAKLAPY DRPINMMFQS YALFPHLDIW ENVAFGLKRE GLPKDEIKQR
VGEMLDLVQL GAYAKRKPHQ LSGGQQQRVA LARSLAKRPK LLLLDEPLGA LDKKLREQTQ
FELVNIIEKV GVTCVMVTHD QEEAMTMASR IAVMSKGRVL QVGSPEEVYE HPANRFVADF
IGNVNIFEGR LSVDEVDRCA AVTGIGEIQV GHGVSGTLNM PVGIAVRPEK IEISKIRPEA
AVNVFTGKVK EIAYFGSYNT YIVVATDGTK VKITEANTSR QDLSDITWED NVFFWWGDRS
GIVLRD
//
