NDVA_BRUA2
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 03-AUG-2022, entry version 111.
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; Proteobacteria; 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=3; 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}.
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DR EMBL; AY237159; AAO84919.1; -; Genomic_DNA.
DR EMBL; AM040264; CAJ10973.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2YQ73; -.
DR SMR; Q2YQ73; -.
DR IntAct; Q2YQ73; 2.
DR STRING; 359391.BAB1_1017; -.
DR EnsemblBacteria; CAJ10973; CAJ10973; BAB1_1017.
DR KEGG; bmf:BAB1_1017; -.
DR PATRIC; fig|359391.11.peg.1730; -.
DR HOGENOM; CLU_000604_84_3_5; -.
DR OMA; MPVLSWW; -.
DR Proteomes; UP000002719; Chromosome I.
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 GO; GO:0043621; F:protein self-association; IPI:AgBase.
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 InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
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 1: Evidence at protein level;
KW 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"
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
