POTA_UREPA
ID POTA_UREPA Reviewed; 519 AA.
AC Q9PR37;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=UU107;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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; AF222894; AAF30513.1; -; Genomic_DNA.
DR RefSeq; WP_006688552.1; NC_002162.1.
DR AlphaFoldDB; Q9PR37; -.
DR SMR; Q9PR37; -.
DR STRING; 273119.UU107; -.
DR EnsemblBacteria; AAF30513; AAF30513; UU107.
DR GeneID; 29672145; -.
DR KEGG; uur:UU107; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_14; -.
DR OMA; IRQKMQV; -.
DR Proteomes; UP000000423; 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; -; 2.
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; 2.
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..519
FT /note="Spermidine/putrescine import ATP-binding protein
FT PotA"
FT /id="PRO_0000286322"
FT DOMAIN 6..401
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT REGION 107..270
FT /note="Insert"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
SQ SEQUENCE 519 AA; 59832 MW; 6912882189F75DD6 CRC64;
MEKTLLHLRD ITKIYDDGFA AVNKFDLKIK KGEFVTLLGP SGCGKTTMLK IIAGFEQPTN
GKILYNGIDI KDMPIRLRPT STVFQDYALF PNMTVKQNIK YGLKLMRKPK DNVDQSIYLQ
ADKVYNSASK KANEKIKELK KQRRGLLAEI KKMDLKYQKN KNIFEIKEMR KNQYLGTLDE
LYQKQGINKN GKPGFLNYFK SWFSHEKLNL NDPIDREIFN LKKAYKEKSG LDKRYDKITY
KYNDLDYWES YWATYPQLKK EQFENKNITR LLTKEEVEKE ANRVINLVGL SARKDSYPSD
LSGGMQQRVA LARSLVIQPE IILLDEPLSA LDAKVRKQLQ DELKKLHKNL GITFILVTHD
QEEALSLSDK VVVMSNGQIE QVGKPSDIYD SPNSLWVANF IGKTNIFEGH YIAKGEVEFD
GITSKTDVIN GFSENEACYI MIRPEDFDVV KKDEGSINAR VESVLYKGLM WDIKCKYNDM
IISVEGVNKV NEGDEIGLDW DDIDVHVIKK DYLNNEQAI