ID Q89W07_BRADU Unreviewed; 254 AA.
AC Q89W07;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:BAC46151.1};
GN OrderedLocusNames=bll0886 {ECO:0000313|EMBL:BAC46151.1};
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:BAC46151.1, 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}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC {ECO:0000256|ARBA:ARBA00005417}.
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DR EMBL; BA000040; BAC46151.1; -; Genomic_DNA.
DR RefSeq; NP_767526.1; NC_004463.1.
DR RefSeq; WP_011083708.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89W07; -.
DR STRING; 224911.AAV28_01280; -.
DR EnsemblBacteria; BAC46151; BAC46151; BAC46151.
DR GeneID; 64020751; -.
DR KEGG; bja:bll0886; -.
DR PATRIC; fig|224911.44.peg.273; -.
DR eggNOG; COG0411; Bacteria.
DR HOGENOM; CLU_000604_1_2_5; -.
DR InParanoid; Q89W07; -.
DR OrthoDB; 8215423at2; -.
DR PhylomeDB; Q89W07; -.
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 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; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR032823; BCA_ABC_TP_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45772:SF3; 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 Pfam; PF12399; BCA_ABC_TP_C; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:BAC46151.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT DOMAIN 5..248
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 254 AA; 27368 MW; DD2B6E3B35F3A0B7 CRC64;
MTLSLETRDL TIRFGGHVAV NNVSCTFRPG ELTAIVGPNG AGKTTYFNLI SGQLRASSGS
ILFDGTDITQ HSAPLRTRAG LGRAFQLTNL FPNLTVEENV RLAVQAANGT HYDMLQPWMV
RRDLIARADA ILDQVALGGR RGVAATALSH GDQRKLEVAL MIALEPKVFM FDEPTAGMSI
DEVPVVLNLI AQLKQDRSKI ILLVEHKMDV VRSLADRIIV LHNGQLVADG VPAEVIASPI
VQEAYLGIAP KSAA
//
