ID   POTA_CLOPS              Reviewed;         349 AA.
AC   Q0SRL2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 92.
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=CPR_1935;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01726};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABG87176.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000312; ABG87176.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q0SRL2; -.
DR   SMR; Q0SRL2; -.
DR   EnsemblBacteria; ABG87176; ABG87176; CPR_1935.
DR   KEGG; cpr:CPR_1935; -.
DR   Proteomes; UP000001824; Chromosome.
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   CDD; cd03300; ABC_PotA_N; 1.
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; IPR017879; PotA_ATP-bd.
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 membrane; Membrane; Nucleotide-binding; Translocase;
KW   Transport.
FT   CHAIN           1..349
FT                   /note="Spermidine/putrescine import ATP-binding protein
FT                   PotA"
FT                   /id="PRO_0000286209"
FT   DOMAIN          7..237
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
SQ   SEQUENCE   349 AA;  39383 MW;  00461338494A6D45 CRC64;
     MKDNNIIELK GITKSYGKDT ILDNLSLNIK KNEFLTLLGP SGCGKTTTLK IIAGFETADS
     GQVVFENNII NDIPPYERQL NTVFQKYALF PHMNVYENIA FGLKLKKIPK DIIDQKVKEM
     LKLVALEGYE NRDIEALSGG QQQRVAIARA LVNEPKVLLL DEPLGALDMK LRKEMQIELK
     KIQQKLGITF IFVTHDQEEA LTMSDTIVVM NKGEIQQMGS PEDIYNEPAN SFVAKFIGES
     NIVDGIMLDD FKVEFGGKIF DCVDKGFEKN EAIEVVIRPE DFEMVKYENG MLKGTVTSII
     FKGVHYEIEV KNENHTWILH NTKHAEIGSK IGLSLDPESI HIMKKESDV