ID A0A2K3V2X5_9DEIO Unreviewed; 379 AA.
AC A0A2K3V2X5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-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=CVO96_15920 {ECO:0000313|EMBL:PNY83132.1};
OS Deinococcus koreensis.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2054903 {ECO:0000313|EMBL:PNY83132.1, ECO:0000313|Proteomes:UP000236379};
RN [1] {ECO:0000313|EMBL:PNY83132.1, ECO:0000313|Proteomes:UP000236379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJW1-2 {ECO:0000313|EMBL:PNY83132.1,
RC ECO:0000313|Proteomes:UP000236379};
RA Choi A.;
RT "Deinococcus koreensis sp. nov., a radiation-resistant bacterium isolated
RT from river water.";
RL Submitted (JAN-2018) 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:PNY83132.1}.
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DR EMBL; PPPD01000001; PNY83132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3V2X5; -.
DR OrthoDB; 9790614at2; -.
DR Proteomes; UP000236379; 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:UP000236379};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU364083};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364083}.
FT DOMAIN 20..255
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 379 AA; 41645 MW; F4A0F00A8C831B70 CRC64;
MSGVAFKGKR VRELSADAAV SVVDVFKSYP AAGGGQTPVL DDIDLDIRQG EFFSLLGPSG
CGKTTLLRIL AGFEQPDAGA VIIGGRDMTG VPPHLRNVNT VFQSYALFPH LNVQENVAFG
LRMKGVPAAA QRERVGRALE SVRIAEFARR RPDQLSGGQR QRVALARAIV NEPQVLLLDE
PLSALDLKLR KELQVELSNL QETLGITFVF VTHDQEEALV MSDRIAVMNR GRVEQLGRAE
ELYERPRTAF VANFLGSSNL IPGTVRELDA TGATVQTVHG PLRTTHARGL TLGQDVTLSV
RPEKLRMERD DETEGNEIRA RVDDIVYTGA ENQYLLEAGG QRLVVFQLNS DIGADEDFDY
EEEVALYLPP DNLIVLEET
//
