ID Q89PU7_BRADU Unreviewed; 260 AA.
AC Q89PU7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=ABC transporter permease protein {ECO:0000313|EMBL:BAC48648.1};
GN OrderedLocusNames=bll3383 {ECO:0000313|EMBL:BAC48648.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC48648.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Involved in beta-(1-->2)glucan export. Transmembrane domains
CC (TMD) form a pore in the inner membrane and the ATP-binding domain
CC (NBD) is responsible for energy generation.
CC {ECO:0000256|ARBA:ARBA00024722}.
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DR EMBL; BA000040; BAC48648.1; -; Genomic_DNA.
DR RefSeq; NP_770023.1; NC_004463.1.
DR RefSeq; WP_011086167.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89PU7; -.
DR STRING; 224911.AAV28_13945; -.
DR EnsemblBacteria; BAC48648; BAC48648; BAC48648.
DR GeneID; 64023131; -.
DR KEGG; bja:bll3383; -.
DR PATRIC; fig|224911.44.peg.3032; -.
DR eggNOG; COG0411; Bacteria.
DR HOGENOM; CLU_000604_1_2_5; -.
DR InParanoid; Q89PU7; -.
DR OrthoDB; 9780942at2; -.
DR PhylomeDB; Q89PU7; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015188; F:L-isoleucine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015192; F:L-phenylalanine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005304; F:L-valine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042941; P:D-alanine transport; IBA:GO_Central.
DR GO; GO:0015808; P:L-alanine transport; IBA:GO_Central.
DR GO; GO:1903806; P:L-isoleucine import across plasma membrane; IBA:GO_Central.
DR GO; GO:1903805; P:L-valine import across plasma membrane; IBA:GO_Central.
DR CDD; cd03219; ABC_Mj1267_LivG_branched; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45772:SF7; AMINO ACID ABC TRANSPORTER ATP-BINDING PROTEIN; 1.
DR PANTHER; PTHR45772; CONSERVED COMPONENT OF ABC TRANSPORTER FOR NATURAL AMINO ACIDS-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT DOMAIN 17..257
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 260 AA; 28325 MW; E04E78D50813430B CRC64;
MDSVAQRLSA VGAGAALELR GVTRLFGALA ALTDVTITVR PGERRAVLGS NGAGKTTLFN
CITGDFPPSS GTIRFFGEDV THFPPYERIR RGLRRTYQIS ALFPGLTVQD NVYLACRGIS
RGRFSFLRPG QNDALMHAAD NLVQAVHLTA VKDQRVAELA HGQQRQLEIA LALAGAPRFV
LFDEPAAGLS PTERQELIEI LTSLPAHIGY IIIEHDMDVA LRVVESVTMM HNGRVFKEGL
PQEIESDPEV QELYLGGGHE
//
