ID A0A220VEA9_9GAMM Unreviewed; 385 AA.
AC A0A220VEA9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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=CF386_06655 {ECO:0000313|EMBL:ASK78697.1};
OS Paraphotobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Paraphotobacterium.
OX NCBI_TaxID=1755811 {ECO:0000313|EMBL:ASK78697.1, ECO:0000313|Proteomes:UP000242175};
RN [1] {ECO:0000313|EMBL:ASK78697.1, ECO:0000313|Proteomes:UP000242175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSCS20N07D {ECO:0000313|EMBL:ASK78697.1,
RC ECO:0000313|Proteomes:UP000242175};
RX PubMed=27154455; DOI=10.1099/ijsem.0.001142;
RA Huang Z., Dong C., Shao Z.;
RT "Paraphotobacterium marinum gen. nov., sp. nov., a member of the family
RT Vibrionaceae, isolated from surface seawater.";
RL Int. J. Syst. Evol. Microbiol. 66:3050-3056(2016).
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; CP022355; ASK78697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220VEA9; -.
DR KEGG; pmai:CF386_06655; -.
DR OrthoDB; 9802264at2; -.
DR Proteomes; UP000242175; Chromosome large.
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 inner membrane {ECO:0000256|ARBA:ARBA00022519};
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:UP000242175};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU364083};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364083}.
FT DOMAIN 15..245
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 385 AA; 44391 MW; 3139A920F5E07B4B CRC64;
MRLKLNRFNP QKNIVSLNNI NKFYGNKLIL NQINLDVFNS EFITILGPSG CGKTTLLRII
AGFEKIDSGQ IIIDDETVNE QVPEKRTVNT VFQSYALFPH MNVFENVAFG LKMKRVKKED
IKTKVINTLK MVQLESYYDK MPSQLSGGQQ QRVAIARAVI NEPKVLLLDE SLSALDYKLR
KRMQLELKQL QRKLGITFIF VTHDQEEALS MSDRIVVLKN GQIEQIGSPK EIYENPNNLF
VAKFIGEINI FDAIVVNRVN DEYILINIES KQKKIKYSKP VKNGQKLKVL LRPEDIKIKE
IKDIKNLDFV DTFLGHVNER TYKGSTLESI IELESGLKIM VSEFFNEDEP DVDHKIGQKV
SVDWIENWEV ILENENENEN NNTIL
//