ID PVDT_PSEE4 Reviewed; 654 AA.
AC Q1I7I9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Pyoverdine export ATP-binding/permease protein PvdT {ECO:0000250|UniProtKB:Q88F88};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q88F88};
GN Name=pvdT {ECO:0000250|UniProtKB:Q88F88}; OrderedLocusNames=PSEEN3665;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
CC -!- FUNCTION: Part of the tripartite efflux system PvdRT-OpmQ required for
CC the secretion into the extracellular milieu of the siderophore
CC pyoverdine (PVD), which is involved in iron acquisition (By
CC similarity). This subunit binds PVD and drives its secretion by
CC hydrolyzing ATP (By similarity). The system is responsible for export
CC of newly synthesized PVD after the final steps of biosynthesis have
CC taken place in the periplasm (By similarity). It is also responsible
CC for recycling of PVD after internalization of ferri-PVD into the
CC periplasm by the outer-membrane receptor FpvA and release of iron from
CC PVD, thus making PVD available for new cycles of iron uptake (By
CC similarity). {ECO:0000250|UniProtKB:Q88F88,
CC ECO:0000250|UniProtKB:Q9I191}.
CC -!- SUBUNIT: Part of the tripartite efflux system PvdRT-OpmQ, which is
CC composed of an inner membrane component with both ATPase and permease
CC domains, PvdT, a periplasmic membrane fusion protein, PvdR, and an
CC outer membrane component, OpmQ. {ECO:0000250|UniProtKB:Q9I191}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q88F88}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide
CC exporter (TC 3.A.1.122) family. {ECO:0000305}.
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DR EMBL; CT573326; CAK16390.1; -; Genomic_DNA.
DR RefSeq; WP_011534771.1; NC_008027.1.
DR AlphaFoldDB; Q1I7I9; -.
DR SMR; Q1I7I9; -.
DR STRING; 384676.PSEEN3665; -.
DR GeneID; 32806723; -.
DR KEGG; pen:PSEEN3665; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_6; -.
DR OrthoDB; 9770036at2; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03255; ABC_MJ0796_LolCDE_FtsE; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003838; ABC3_permease_dom.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR017911; MacB-like_ATP-bd.
DR InterPro; IPR025857; MacB_PCD.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR30572:SF14; MACROLIDE EXPORT ATP-BINDING_PERMEASE PROTEIN MACB; 1.
DR PANTHER; PTHR30572; MEMBRANE COMPONENT OF TRANSPORTER-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF02687; FtsX; 1.
DR Pfam; PF12704; MacB_PCD; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51267; MACB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..654
FT /note="Pyoverdine export ATP-binding/permease protein PvdT"
FT /id="PRO_0000280173"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 6..245
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 654 AA; 69628 MW; EF96C8CB11B25740 CRC64;
MSAPLIELCD IRKAYGGIDS PKVEVLRGIS LSIHPGEFVA IVGASGSGKS TLMNILGCLD
RPTSGSYRFA GRDVAELDSD ELAWLRREAF GFVFQGYHLI PSGSAQENVE MPAIYAGTPP
AERHARALAL LDRLGLASRT GNRPHQLSGG QQQRVSIARA LMNGGHIILA DEPTGALDSH
SGAEVMALLD ELASQGHVII LITHDREVAA RAQRIIEIRD GQMVSDSAAS QPSPAQPEQL
QANDLRQRLD RGAILKGAWK GEMIEALQAA WRVMWINRFR TALTLLGIII GVASVVVMLA
VGEGSKRQVM AQMAAFGSNI LYLNGKRATA QEPGGIVTLD DVAAIGELPQ VLHVMPVIGG
QLMVRQGNSS QKFYVGGNNT WFPAIFNWPV VEGTFFSEAD EASGAAVAVI GQKVRSKMFG
EGSNPLGQYL LIGNVPFQVV GILAAKGASS GSEDSDERIV VPYSAASIRL FGSHDPEYVA
IAAIDSRRVN ETEAAIDRLL RQRHQGKHDF DLTNDAALIQ AEARTQNSLS LMLGAIAAIS
LLVGGIGVMN IMLMTVRERT REIGIRMATG ARQRDILRQF LTEAVMLSMV GGVTGIVIAL
LVGGGLLLAD IAVAFALPAI LGAFACAVIT GVVFGFMPAR KAARLDPVKA LTSE
//
