ID NDVA_BRUA2 Reviewed; 599 AA. AC Q2YQ73; Q57DD0; Q844Y8; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 119. 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}; Synonyms=cgt; GN OrderedLocusNames=BAB1_1017; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BETA-(1->2)GLUCAN TRANSPORT, RP AND SUBCELLULAR LOCATION. RX PubMed=15039351; DOI=10.1128/iai.72.4.2263-2271.2004; RA Roset M.S., Ciocchini A.E., Ugalde R.A., Inon de Iannino N.; RT "Molecular cloning and characterization of cgt, the Brucella abortus cyclic RT beta-1,2-glucan transporter gene, and its role in virulence."; RL Infect. Immun. 72:2263-2271(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). CC -!- FUNCTION: Involved in beta-(1-->2)glucan export. Its export to the CC periplasmic space is required to exert its action as a virulence CC factor. Transmembrane domains (TMD) form a pore in the inner membrane CC and the ATP-binding domain (NBD) is responsible for energy generation CC (Probable). {ECO:0000305|PubMed:15039351}. 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 -!- INTERACTION: CC Q2YQ73; Q2YNV7: BAB1_0108; NbExp=5; IntAct=EBI-11509336, EBI-11509311; CC Q2YQ73; Q2YRC8: BAB1_1718; NbExp=4; IntAct=EBI-11509336, EBI-11509356; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01728, ECO:0000269|PubMed:15039351}; Multi-pass membrane CC protein {ECO:0000255|HAMAP-Rule:MF_01728, ECO:0000269|PubMed:15039351}. 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; AY237159; AAO84919.1; -; Genomic_DNA. DR EMBL; AM040264; CAJ10973.1; -; Genomic_DNA. DR PDB; 7ZNU; EM; 4.00 A; A/B=1-599. DR PDB; 7ZO8; EM; 3.60 A; A/B=1-599. DR PDB; 7ZO9; EM; 3.50 A; A/B=1-599. DR PDB; 7ZOA; EM; 4.00 A; A/B=1-599. DR PDBsum; 7ZNU; -. DR PDBsum; 7ZO8; -. DR PDBsum; 7ZO9; -. DR PDBsum; 7ZOA; -. DR AlphaFoldDB; Q2YQ73; -. DR EMDB; EMD-14814; -. DR EMDB; EMD-14843; -. DR EMDB; EMD-14844; -. DR EMDB; EMD-14845; -. DR SMR; Q2YQ73; -. DR IntAct; Q2YQ73; 2. DR STRING; 359391.BAB1_1017; -. DR KEGG; bmf:BAB1_1017; -. DR PATRIC; fig|359391.11.peg.1730; -. DR HOGENOM; CLU_000604_84_3_5; -. DR Proteomes; UP000002719; 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 GO; GO:0043621; F:protein self-association; IPI:AgBase. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane; KW Nucleotide-binding; Reference proteome; Sugar transport; Translocase; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..599 FT /note="Beta-(1-->2)glucan export ATP-binding/permease FT protein NdvA" FT /id="PRO_0000290245" 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" FT HELIX 2..14 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 18..45 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 57..100 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 104..110 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 114..153 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 156..202 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 205..209 FT /evidence="ECO:0007829|PDB:7ZO9" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 214..230 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 233..263 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 271..313 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 322..325 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 335..341 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 364..367 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 375..381 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 388..394 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 399..401 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 404..409 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 410..414 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 422..424 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 425..430 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 432..436 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 438..447 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 450..454 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 457..459 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 467..469 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 475..488 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 491..497 FT /evidence="ECO:0007829|PDB:7ZO9" FT TURN 498..501 FT /evidence="ECO:0007829|PDB:7ZO9" FT HELIX 504..518 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 521..526 FT /evidence="ECO:0007829|PDB:7ZO9" FT TURN 530..535 FT /evidence="ECO:0007829|PDB:7ZO9" FT STRAND 537..545 FT /evidence="ECO:0007829|PDB:7ZO9" 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 //