NDVA_RHIL3
ID NDVA_RHIL3 Reviewed; 587 AA.
AC Q1MAB5;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
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}; OrderedLocusNames=RL4640;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
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; AM236080; CAK10123.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1MAB5; -.
DR SMR; Q1MAB5; -.
DR STRING; 216596.RL4640; -.
DR EnsemblBacteria; CAK10123; CAK10123; RL4640.
DR KEGG; rle:RL4640; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_8_5; -.
DR OMA; MPVLSWW; -.
DR Proteomes; UP000006575; Chromosome.
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..587
FT /note="Beta-(1-->2)glucan export ATP-binding/permease
FT protein NdvA"
FT /id="PRO_0000290251"
FT TRANSMEM 23..43
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 128..148
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 587 AA; 64762 MW; 519413311A574D37 CRC64;
MTLFKVYARA LRYLGAYKLR VSLVVVANIV LATITIAEPI LFGRIIDAIS GKGEVKPILF
MWATFAVFNT IAFVLVAREA DRLAHGRRAT LLTEAFGRII SMPLGWHHQR GTSNALHTLL
RACETLFGLW LEFMRNHLST VIALALLIPT AMSMDLRLSA VLMVLAIAYW LIGRVVMSRT
KDGQASVENH YHTVFSHVSD SISNVSVLHS YNRIEAETRA LKSFADRLLE AQYPVLDWWA
IASALNRMAS TIAMMVVLII GTMLVQAGQL RVGDVIAFIG FANLLIGRLD LMRQFATQIF
EARSKLEEFY ALEDSVRERE EPAGNGEIKD VKGAIEFRDV SFGFGNSSQG LHNVSFSVKA
GQTVAIVGPT GAGKTTLVNL LQRVYDAQGG KILVDGTDIT KVTRKSLRRH IATVFQDAGL
LNRSISDNIR LGREGASEEE MRRAAEAAAA ADFIETREDR YDTHVGERGN KLSGGERQRI
AIARAILKDA PILVLDEATS ALDVETEARV KAAIDNLRQN RTTFIIAHRL STVREADMVL
FLDDGRVVEQ GSFDELSHSN GRFAALLRAS GILTDEEVRK AHTTEAA
