POTA_HAEI8
ID POTA_HAEI8 Reviewed; 372 AA.
AC Q4QK57;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=NTHI1820;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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=AAX88590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000057; AAX88590.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_005650696.1; NC_007146.2.
DR AlphaFoldDB; Q4QK57; -.
DR SMR; Q4QK57; -.
DR EnsemblBacteria; AAX88590; AAX88590; NTHI1820.
DR GeneID; 66614473; -.
DR KEGG; hit:NTHI1820; -.
DR HOGENOM; CLU_000604_1_1_6; -.
DR Proteomes; UP000002525; 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; Translocase; Transport.
FT CHAIN 1..372
FT /note="Spermidine/putrescine import ATP-binding protein
FT PotA"
FT /id="PRO_0000286223"
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 372 AA; 42362 MW; 2980CB13CAC76B32 CRC64;
MENQPQNKPI IELRSIKKSY GSNTIINDFN LAINNGEFVT ILGPSGCGKT TVLRLLAGLE
ELDSGSIILD GEDITNVPAE KRHINTVFQS YALFPHMTIF ENVAFGLRMQ KVPNEEIKPR
VLEALRMVQL EEMADRKPTQ LSGGQQQRIA IARAVVNKPK VLLLDESLSA LDYKLRKQMQ
QELKMLQRQL GITFIFVTHD QEEAITMSDR IVLLRKGKIA QDGSPREIYE DPANLFVARF
IGEINVFEAT VIERKSEQVV LANVEGRICD IYTDMPVEKD QKLQVLLRPE DIVIEELDEN
EHSKAIIGHI IDRTYKGMTL ESTVEFDHNG MRVLVSEFFN EDDPHMDHSI GQRVGITWHE
GWEVVLNDED NQ