ID POTA_STRSV Reviewed; 385 AA.
AC A3CMQ7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=SSA_1048;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN44462.1; -; Genomic_DNA.
DR RefSeq; WP_011836889.1; NC_009009.1.
DR RefSeq; YP_001035012.1; NC_009009.1.
DR AlphaFoldDB; A3CMQ7; -.
DR SMR; A3CMQ7; -.
DR STRING; 388919.SSA_1048; -.
DR KEGG; ssa:SSA_1048; -.
DR PATRIC; fig|388919.9.peg.994; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_9; -.
DR OrthoDB; 9790614at2; -.
DR Proteomes; UP000002148; 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 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; IPR013611; Transp-assoc_OB_typ2.
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.
DR PROSITE; PS51305; POTA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..385
FT /note="Spermidine/putrescine import ATP-binding protein
FT PotA"
FT /id="PRO_0000286314"
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 385 AA; 44268 MW; 096D62D4154F522D CRC64;
MKKPIIEFKN VSKVFEDNNT VVLKDINFEL EEGKFYTLLG SSGSGKSTIL NIIAGLLDAT
DGDIFLDGVR INDIPTNKRD VHTVFQSYAL FPHMNVFENV AFPLRLRKVD KKEIQERVTE
VLKMVQLEGF ERRSIRKLSG GQRQRVAIAR AIINQPRVVL LDEPLSALDL KLRTDMQYEL
RELQQRLGIT FVFVTHDQEE ALAMSDWIFV MNDGEIVQSG TPVDIYDEPI NHFVATFIGE
SNILPGKMIE DYLVEFNGKR FEAVDGGMRP NESVEVVIRP EDLRITLPEE GKLQVKVDTQ
LFRGVHYEII AYDELGNEWM IHSTRKAIVG EEIGLHFEPE DIHIMRLNET EEEFDARIEE
YVEVEEQEAG LINAIEEERD EENNL
//
