POTA_PASMU
ID POTA_PASMU Reviewed; 370 AA.
AC Q9CP06;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
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=PM0264;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01726}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK02348.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004439; AAK02348.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_005724659.1; NC_002663.1.
DR AlphaFoldDB; Q9CP06; -.
DR SMR; Q9CP06; -.
DR STRING; 747.DR93_1796; -.
DR EnsemblBacteria; AAK02348; AAK02348; PM0264.
DR GeneID; 62226226; -.
DR KEGG; pmu:PM0264; -.
DR HOGENOM; CLU_000604_1_1_6; -.
DR OMA; IHVMRFN; -.
DR Proteomes; UP000000809; 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 inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..370
FT /note="Spermidine/putrescine import ATP-binding protein
FT PotA"
FT /id="PRO_0000286270"
FT DOMAIN 11..241
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
SQ SEQUENCE 370 AA; 41923 MW; F2ABFB67293FDECD CRC64;
MESSVQNKPI IELRSITKSY GDKTIIENFN LTINNGEFLT ILGPSGCGKT TVLRLLAGLE
ELDSGNIILD GEDITHVPAE QRHVNTVFQS YALFPHMTIF ENVAFGLRMQ KVPNEEIKPR
VLEALRMVQL EEYAYSKPAQ LSGGQQQRIA IARAVVNKPK VLLLDESLSA LDYKLRKQMQ
NELKALQRKL GITFIFVTHD QEEALTMSDR IIVLRKGHIQ QDGSPREIYE EPKNLFVAKF
IGEINIFNAT VLTRVDEKRV RANVEGRVCD IYTNLDVVAE QKLKVLLRPE DILIEELDEN
QSSKAIIGHV ADRNYKGMTL ESNITLDHNG MTVLVSEFFN EDDPNIDHSL GQKVALTWHE
GWEVVLSDEE