ID   POTA_STRP8              Reviewed;         384 AA.
AC   Q7CN92;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=spyM18_1064;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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}.
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DR   EMBL; AE009949; AAL97688.1; -; Genomic_DNA.
DR   RefSeq; WP_010922284.1; NC_003485.1.
DR   AlphaFoldDB; Q7CN92; -.
DR   SMR; Q7CN92; -.
DR   KEGG; spm:spyM18_1064; -.
DR   HOGENOM; CLU_000604_1_1_9; -.
DR   OMA; IHVMRFN; -.
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; 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; 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 membrane; Membrane; Nucleotide-binding; Translocase;
KW   Transport.
FT   CHAIN           1..384
FT                   /note="Spermidine/putrescine import ATP-binding protein
FT                   PotA"
FT                   /id="PRO_0000286308"
FT   DOMAIN          6..238
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
SQ   SEQUENCE   384 AA;  43822 MW;  4B43ED238A64D446 CRC64;
     MTKPIITFNN VSKTFEDSGT QVLKNINFDL EEGKFYTLLG ASGSGKSTIL NIMAGLLDAS
     SGDIYLDGER INDLPINKRD IHTVFQNYAL FPHMTVFENV AFALKLKKVD KKEIAKRVKE
     TLKMVQLEGF ENRSIQKLSG GQRQRVAIAR AIINQPRVVL LDEPLSALDL KLRTEMQYEL
     RELQQRLGIT FVFVTHDQEE ALAMSDWIFV MNEGEIVQSG TPVDIYDEPI NHFVANFIGE
     SNIINGTMIE DYLVSFNGKE FESVDGGMRP NEPVEVVIRP EDLQITLPEE GKLQVKVDTQ
     LFRGVHYEII AYDELGNEWM IHSTRKAIEG EVIGLDFTPE DLHIMRLNET EEEFDARIEE
     YVEMDEPEDG LINAIEEERN EENL