ID   POTA_RUEPO              Reviewed;         366 AA.
AC   Q5LT05;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Spermidine/putrescine import ATP-binding protein PotA {ECO:0000255|HAMAP-Rule:MF_01726};
DE            EC=7.6.2.11 {ECO:0000255|HAMAP-Rule:MF_01726};
GN   Name=potA {ECO:0000255|HAMAP-Rule:MF_01726}; OrderedLocusNames=SPO1609;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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:0000255|HAMAP-Rule:MF_01726}.
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:0000255|HAMAP-Rule:MF_01726};
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:0000255|HAMAP-Rule:MF_01726}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01726}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01726}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Spermidine/putrescine importer (TC 3.A.1.11.1) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01726}.
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DR   EMBL; CP000031; AAV94896.1; -; Genomic_DNA.
DR   RefSeq; WP_011047346.1; NC_003911.12.
DR   AlphaFoldDB; Q5LT05; -.
DR   SMR; Q5LT05; -.
DR   STRING; 246200.SPO1609; -.
DR   EnsemblBacteria; AAV94896; AAV94896; SPO1609.
DR   KEGG; sil:SPO1609; -.
DR   eggNOG; COG3842; Bacteria.
DR   HOGENOM; CLU_000604_1_1_5; -.
DR   OMA; IADNEFF; -.
DR   OrthoDB; 1200451at2; -.
DR   Proteomes; UP000001023; 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   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005893; Sp_pt_ABC_ATP-bd.
DR   InterPro; IPR013611; Transp-assoc_OB_typ2.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08402; TOBE_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; SSF50331; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01187; potA; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51305; POTA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..366
FT                   /note="Spermidine/putrescine import ATP-binding protein
FT                   PotA"
FT                   /id="PRO_0000286288"
FT   DOMAIN          14..247
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT   BINDING         49..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
SQ   SEQUENCE   366 AA;  39837 MW;  03518ED897D7A756 CRC64;
     MVPPTGERSL TKAISARALR KVYPGTPPVE ALGGVDIDIA DNEFFTLLGP SGCGKTTILR
     LIAGFEHPTS GSLDMFGQSL LDLPPYKRQI NTVFQSYALF PHMSVAENIG FGLEMLGKPK
     SEIKSTVAEM MDLVQMSHLA DRQTSQISGG QQQRVALARA LAPKPRVLLL DEPLSALDFK
     LRKNMQLELK RLQTETGITF IFVTHDQEEA LTMSDRIAVM SDGAIRQIGS PRDIYDHPAD
     RFVADFIGDT NFLPADVIAT EGERVSLRLG SGKTITAPAR HAGGGRVTLA VRPEHARLEA
     EDSGLLPGVL SDAVYFGTDT HFHIALDDGT AFVLRQQNSP DTETRFAKGE RVSVSFPGEV
     AQVLRD