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Database: UniProt
Entry: H0TNI0_9BRAD
LinkDB: H0TNI0_9BRAD
Original site: H0TNI0_9BRAD 
ID   H0TNI0_9BRAD            Unreviewed;       258 AA.
AC   H0TNI0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Leucine/isoleucine/valine transporter subunit ATP-binding component of ABC superfamily {ECO:0000313|EMBL:CCE08018.1};
GN   Name=livG {ECO:0000313|EMBL:CCE08018.1};
GN   ORFNames=BRAS3843_2520033 {ECO:0000313|EMBL:CCE08018.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE08018.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
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:CCE08018.1}.
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DR   EMBL; CAFK01000171; CCE08018.1; -; Genomic_DNA.
DR   RefSeq; WP_008970533.1; NZ_CAFK01000171.1.
DR   AlphaFoldDB; H0TNI0; -.
DR   OrthoDB; 9779872at2; -.
DR   Proteomes; UP000002686; 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; 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: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   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:CCE08018.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002686}.
FT   DOMAIN          6..253
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   258 AA;  27628 MW;  57C858D234EFD9A7 CRC64;
     MAEAALRVDK VAMHFGGLVA ISDMTFVVGE GEIVSLIGPN GAGKTTAFNV VTGFLTPTHG
     EVSYRGQVLT GLKPQQIASL GLVRTFQRTS VFPNDTVYQN VVIGLHRRGK ATLLSSILGL
     PGARQSEAAS RREAVQLIEW IGLGRRAHDL AGSLSYGEQR LVGVAVALAA EPSMLLLDEP
     VSGMNASETH TFVQLIRKLR DRGITILLVE HDMPMVMSVS DRIVVLNYGR IIAEGPPDAI
     RNDPAVIEAY LGQGVKHA
//
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