ID A0A1H5J4U0_9ACTN Unreviewed; 381 AA.
AC A0A1H5J4U0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN05216533_2431 {ECO:0000313|EMBL:SEE47509.1};
OS Streptomyces sp. Ag109_O5-10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEE47509.1, ECO:0000313|Proteomes:UP000198812};
RN [1] {ECO:0000313|EMBL:SEE47509.1, ECO:0000313|Proteomes:UP000198812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEE47509.1,
RC ECO:0000313|Proteomes:UP000198812};
RA de Groot N.N.;
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; FNTQ01000001; SEE47509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5J4U0; -.
DR STRING; 1855349.SAMN05216533_2431; -.
DR OrthoDB; 9802264at2; -.
DR Proteomes; UP000198812; Unassembled WGS sequence.
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 GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03300; ABC_PotA_N; 1.
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; IPR017879; PotA_ATP-bd.
DR InterPro; IPR013611; Transp-assoc_OB_typ2.
DR NCBIfam; TIGR01187; potA; 1.
DR PANTHER; PTHR42781; SPERMIDINE/PUTRESCINE IMPORT ATP-BINDING PROTEIN POTA; 1.
DR PANTHER; PTHR42781:SF4; 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:UP000198812};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU364083};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364083}.
FT DOMAIN 9..238
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 381 AA; 40978 MW; 9DB776B93C81C5F3 CRC64;
MTTDSSGDVR LTGIGKTYDN GFTAVQPMDL TVPQGSFFAL LGASGCGKTT TLRMIAGLEE
PTTGTVHLGD QDVTHLPPYK RPVNTVFQSY ALFPHLDIFE NVAFGLRRRG IKSVKKQVED
MLELVQLGEQ ARKKPHQLSG GQQQRVAVAR ALINHPKVLL LDEPLGALDL KLRRQMQLEL
KRIQTEVGIT FVHVTHDQEE AMTMADTVAV MNAGRVEQLG SPADLYENPN TTFVANFLGT
SNLIEAEVDS KSGDDIVLKA GGGKLVLPEA RCSAPTTTGG KVLVGVRPEK ISLTHADDAG
SIPEGRNRIT GKVADASFIG VSTQYVIDSA VCPEFAVYVQ NVERDGRLVP GADVVLHWSP
AHTFGLDAAQ DIDAGTEEEA A
//