ID Q89C67_BRADU Unreviewed; 252 AA.
AC Q89C67;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:BAC53195.1};
GN OrderedLocusNames=bll7930 {ECO:0000313|EMBL:BAC53195.1};
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:BAC53195.1, 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; BAC53195.1; -; Genomic_DNA.
DR RefSeq; NP_774570.1; NC_004463.1.
DR RefSeq; WP_011090654.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89C67; -.
DR STRING; 224911.AAV28_37370; -.
DR EnsemblBacteria; BAC53195; BAC53195; BAC53195.
DR GeneID; 64027678; -.
DR KEGG; bja:bll7930; -.
DR PATRIC; fig|224911.44.peg.8079; -.
DR eggNOG; COG0411; Bacteria.
DR HOGENOM; CLU_000604_1_2_5; -.
DR InParanoid; Q89C67; -.
DR OrthoDB; 9779872at2; -.
DR PhylomeDB; Q89C67; -.
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; IPR032823; BCA_ABC_TP_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45772:SF1; 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; PS50893; ABC_TRANSPORTER_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:BAC53195.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT DOMAIN 4..252
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 252 AA; 28383 MW; E2A026780CA271C1 CRC64;
MSYFRAENLS LHFGGLKAVD AVSFAVEKGE ILSIIGPNGA GKSSIFNLIS RIYRPTSGRI
FFEDQDITEQ PPYDIARLGI ARTFQNIELF ENATVLSNLL VGRHRHSTTQ LWQELLFLPS
VRANEKLHRR RVEQVIEFLD LEPYRDKLIS GLPYGVRKVI ELARALCSEP KLILLDEPSS
GLNVEETDDM SFWIRDMKNE LGVTVLMVEH DMSLVNRVSD RVIALNYGRV LAMGSPAEVQ
QHPDVVAAYL GA
//
