ID   NDVA_AGRVI              Reviewed;         584 AA.
AC   Q71ED1;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Beta-(1-->2)glucan export ATP-binding/permease protein NdvA {ECO:0000255|HAMAP-Rule:MF_01728};
DE            EC=7.5.2.3 {ECO:0000255|HAMAP-Rule:MF_01728};
GN   Name=ndvA {ECO:0000255|HAMAP-Rule:MF_01728};
OS   Agrobacterium vitis (Rhizobium vitis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=F2/5;
RX   PubMed=12848431; DOI=10.1094/mpmi.2003.16.7.650;
RA   Zheng D., Zhang H., Carle S., Hao G., Holden M.R., Burr T.J.;
RT   "A luxR homolog, aviR, in Agrobacterium vitis is associated with induction
RT   of necrosis on grape and a hypersensitive response on tobacco.";
RL   Mol. Plant Microbe Interact. 16:650-658(2003).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->2)-beta-D-glucosyl](n)(in) + ATP + H2O = [(1->2)-beta-D-
CC         glucosyl](n)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:18453,
CC         Rhea:RHEA-COMP:11881, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:27517, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.5.2.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01728};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01728}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01728}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01728}.
CC   -!- DOMAIN: In NdvA the ATP-binding domain (NBD) and the transmembrane
CC       domain (TMD) are fused.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Beta-
CC       (1-->2)glucan exporter (TC 3.A.1.108.1) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01728}.
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DR   EMBL; AF521015; AAQ08607.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q71ED1; -.
DR   SMR; Q71ED1; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015441; F:ABC-type beta-glucan transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR005896; NdvA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   TIGRFAMs; TIGR01192; chvA; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51317; NDVA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Sugar transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..584
FT                   /note="Beta-(1-->2)glucan export ATP-binding/permease
FT                   protein NdvA"
FT                   /id="PRO_0000290238"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   DOMAIN          21..301
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   DOMAIN          335..569
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   BINDING         368..375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
SQ   SEQUENCE   584 AA;  64210 MW;  AF37D2E0B91D9728 CRC64;
     MSLLQIYWRA LQYLAAYRLK VSLVVAANII LAVITIAEPI LFGWIIDAIS SGKPDKDILF
     LWGGFGIFNT IAFVLVAREA DRLAHGRRAS LLTEAFGRII SMPLSWHHQR GTSNALHTLL
     RASETLFGLW LEFMRTHLAT AVALVLLVPT AFSMDVRLTL VLIVLGLIYV AIGKMVMDKT
     KDGQASVESH YHTVFSHVSD TISNVSVVHS YNRIQAETSA LKTFTSKLLD AQYPVLDWWA
     IASGLNRIAS TASMLIILII GTMLVQSGEL RVGDVIAFIG FANLLIARLD QMRQFSTQIF
     EARAKLEDFY VLEDSVQDRD EPVGNRDLKS VRGDVEFRHV SFDFANTTQG VKDVSFTVKA
     GQTIAIVGPT GAGKTTLINL LQRVHEPQQG QILIDGADIS TITRQSLRNS IATVFQDAGI
     LNRSIADNIR IGRENATDED IVKAAEAAAA TDFIESRLSG FDTDVGERGN RLSGGERQRI
     AIARAILKDA PILVLDEATS ALDVETEERV KSAIDRLRQN RTTFIIAHRL STVREADQVL
     FLDHGRIVEM GGYDELSAKG GRFAALLHTS GLLNDDDKTA VKVG