ID A0A0Q6AGM2_9BRAD Unreviewed; 248 AA.
AC A0A0Q6AGM2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:KQT29104.1};
GN ORFNames=ASG57_00185 {ECO:0000313|EMBL:KQT29104.1};
OS Bradyrhizobium sp. Leaf396.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT29104.1, ECO:0000313|Proteomes:UP000051536};
RN [1] {ECO:0000313|EMBL:KQT29104.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT29104.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT29104.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT29104.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQT29104.1}.
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DR EMBL; LMQJ01000001; KQT29104.1; -; Genomic_DNA.
DR RefSeq; WP_024338162.1; NZ_LMQJ01000001.1.
DR AlphaFoldDB; A0A0Q6AGM2; -.
DR OrthoDB; 9776369at2; -.
DR Proteomes; UP000051536; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03224; ABC_TM1139_LivF_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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43820; HIGH-AFFINITY BRANCHED-CHAIN AMINO ACID TRANSPORT ATP-BINDING PROTEIN LIVF; 1.
DR PANTHER; PTHR43820:SF4; HIGH-AFFINITY BRANCHED-CHAIN AMINO ACID TRANSPORT ATP-BINDING PROTEIN LIVF; 1.
DR Pfam; PF00005; ABC_tran; 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:KQT29104.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 20..248
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 248 AA; 27025 MW; 8A84106979B9DE34 CRC64;
MPDTAIAEAP AMATTGGNIL QVRNLEAWYG ESHILHGINF DVNAGEVVTL LGRNGAGKTT
TLKSIMGIIG KRSGSVKFND QEIIRATSDK IARMGIAFCP EERGIFSSLD VRENLMLPPV
VREGGLPLDQ IFELFPNLKE RLGSQGTKLS GGEQQMLAIA RILRTGASFL MLDEPTEGLA
PVIIQQIGHT IARLKKEGFT ILLVEQNFRF ASTVADRYYV VEHGKIIDGF SNAELAANMD
KLHTYLGV
//
