ID A0A254QWB1_9RHOB Unreviewed; 358 AA.
AC A0A254QWB1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ATO1_03715 {ECO:0000313|EMBL:OWU82013.1};
OS Phaeobacter sp. 22II1-1F12B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU82013.1, ECO:0000313|Proteomes:UP000197279};
RN [1] {ECO:0000313|EMBL:OWU82013.1, ECO:0000313|Proteomes:UP000197279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU82013.1,
RC ECO:0000313|Proteomes:UP000197279};
RA Lai Q., Li G., Shao Z.;
RT "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL Submitted (APR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWU82013.1}.
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DR EMBL; AQQP01000002; OWU82013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254QWB1; -.
DR OrthoDB; 9802264at2; -.
DR Proteomes; UP000197279; 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; 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:UP000197279};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU364083};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364083}.
FT DOMAIN 4..234
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 358 AA; 38317 MW; C6A8882F1C48A197 CRC64;
MSSVTLKNIV KRFGTFTAVH QANLEIPEGD FVTLLGPSGC GKTTNLRMIA GLLDPTEGEI
QIGGKRVNDI PIHKRNLGIV FQNYALFPHK TVAENVAFGL KYRDVPKSEV ASRVQAALDL
VQLPDVGDRY PKALSGGQQQ RIALARAIVI EPDVLLLDEP LSALDANLRE DMRVELKRIQ
SQIGVTTVFV THDQSEALAM SDKIVVMSAG RIEQVGTPEE VYNTPASEFV ANFLGASNIL
NGTCLGKTGS DVAVETPLFG SVPVPAGKAS GLDHGPAKLV LRSEKLTLLA PGADTTGMIT
APATVETVDY QGQTVRYFIR MGDTQLQAIN LIDERPFPEG TEVTAAFRAK DCAALPGA
//
