POTA_LAWIP
ID POTA_LAWIP Reviewed; 368 AA.
AC Q1MQ44;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=LI0829;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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; AM180252; CAJ54883.1; -; Genomic_DNA.
DR RefSeq; WP_011526912.1; NC_008011.1.
DR AlphaFoldDB; Q1MQ44; -.
DR SMR; Q1MQ44; -.
DR STRING; 363253.LI0829; -.
DR KEGG; lip:LI0829; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_7; -.
DR OMA; MADRMMI; -.
DR OrthoDB; 1200451at2; -.
DR Proteomes; UP000002430; 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; 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; 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;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..368
FT /note="Spermidine/putrescine import ATP-binding protein
FT PotA"
FT /id="PRO_0000286238"
FT DOMAIN 8..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 368 AA; 41304 MW; 112D69C5A98588DA CRC64;
MTGKGCIIEL KNVSKIFEDT CALDNINLQI ANGEFLTLLG PSGCGKTTIL RIISGFETPD
VGEILIAGVN VSGFPPERRQ VNTVFQHYAL FPHMTVRDNV AFGLRMQKCP REKVNELVFE
ALRMVHLENF ADRRPSQLSG GQQQRVAIAR AVVNKPLLLL LDEPFSALDH KLRQIMQLEI
KHLQRKLGIT FVFVTHDQEE AFAMSDRVVV MNQGRIEQIG TPQCIYEEPV NLFVARFVGE
INNLAGTILS CNDEGIYEAA IANEVFPLRT PHRFSPGEAV NVLLRPEDIR IYLLDEEVLK
VPHLRGRIEE TVYKGATVDI IIALDVGGTL RVAEFFNEDD AEISYNEGER VAVTWVDGWE
VVLPHEMA