ID NDVA_BRUAB Reviewed; 599 AA. AC P0C529; Q57DD0; Q844Y8; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 92. 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}; GN OrderedLocusNames=BruAb1_1004; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison to RT the highly similar genomes of Brucella melitensis and Brucella suis."; RL J. Bacteriol. 187:2715-2726(2005). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017223; AAX74354.1; -; Genomic_DNA. DR AlphaFoldDB; P0C529; -. DR SMR; P0C529; -. DR EnsemblBacteria; AAX74354; AAX74354; BruAb1_1004. DR KEGG; bmb:BruAb1_1004; -. DR HOGENOM; CLU_000604_84_3_5; -. DR Proteomes; UP000000540; Chromosome I. 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 GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR CDD; cd18562; ABC_6TM_NdvA_beta-glucan_exporter_like; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR039421; Type_1_exporter. DR NCBIfam; TIGR01192; chvA; 1. DR PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1. DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..599 FT /note="Beta-(1-->2)glucan export ATP-binding/permease FT protein NdvA" FT /id="PRO_0000290244" FT TRANSMEM 22..42 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728" FT TRANSMEM 55..75 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728" FT TRANSMEM 156..176 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 276..296 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 599 AA; 65951 MW; 2626C3220E57341C CRC64; MSLLKIYWRA MQYLAVERTA TITMCVASVL VALVTLAEPV LFGRVIQSIS DKGDIFSPLL MWAALGGFNI MAAVFVARGA DRLAHRRRLG VMIDSYERLI TMPLAWHQKR GTSNALHTLI RATDSLFTLW LEFMRQHLTT VVALATLIPV AMTMDMRMSL VLIVLGVIYV MIGQLVMRKT KDGQAAVEKH HHKLFEHVSD TISNVSVVQS YNRIASETQA LRDYAKNLEN AQFPVLNWWA LASGLNRMAS TFSMVVVLVL GAYFVTKGQM RVGDVIAFIG FAQLMIGRLD QISAFINQTV TARAKLEEFF QMEDATADRQ EPENVADLND VKGDIVFDNV TYEFPNSGQG VYDVSFEVKP GQTVAIVGPT GAGKTTLINL LQRVFDPAAG RIMIDGTDTR TVSRRSLRHA IATVFQDAGL FNRSVEDNIR VGRANATHEE VHAAAKAAAA HDFILAKSEG YDTFVGERGS QLSGGERQRL AIARAILKDS PILVLDEATS ALDVETEEKV TQAVDELSHN RTTFIIAHRL STVRSADLVL FMDKGHLVES GSFNELAERG GRFSDLLRAG GLKLEDKQPK QPVVEGSNVM PFPVKGAVA //