POTA_STRMU
ID POTA_STRMU Reviewed; 384 AA.
AC Q8DUF7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=SMU_973;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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; AE014133; AAN58676.1; -; Genomic_DNA.
DR RefSeq; NP_721370.1; NC_004350.2.
DR RefSeq; WP_002262837.1; NC_004350.2.
DR AlphaFoldDB; Q8DUF7; -.
DR SMR; Q8DUF7; -.
DR STRING; 210007.SMU_973; -.
DR EnsemblBacteria; AAN58676; AAN58676; SMU_973.
DR GeneID; 66817608; -.
DR KEGG; smu:SMU_973; -.
DR PATRIC; fig|210007.7.peg.867; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_9; -.
DR OMA; IHVMRFN; -.
DR PhylomeDB; Q8DUF7; -.
DR Proteomes; UP000002512; 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; 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; 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 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..384
FT /note="Spermidine/putrescine import ATP-binding protein
FT PotA"
FT /id="PRO_0000286301"
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; 43534 MW; 76421029E26E0223 CRC64;
MTKPIIAFKN VSKVFEDNGT VVLKNINFEL EEGKFYTLLG ASGSGKSTIL NLIAGLLEAS
SGGIFLDGKR INDIPINKRD VHTVFQSYAL FPHMTVFENV AFPLKLRKVA KKEIEKRVTE
ALNMVRLAGF EKRSIGKLSG GQRQRVAIAR AIINQPKVVL LDEPLSALDL KLRTEMQYEL
RDLQQRLGIT FVFVTHDQEE ALAMSDWIFV MNDGEIVQSG TPVDIYDEPI NHFVATFIGE
SNILPAVMIE DYLVEFNGKR FEAVDGGMRP NEAVEVVIRP EDLQITLPEE GKLQVKVETQ
LFRGVHYEII AHDELGNEWM IHSTHKAIEG EIIGLDFTPE DIHIMRLNET EAEFDARIEE
YVETEEHEEG LINAIEEERH EEES