NDVA_RHIME
ID NDVA_RHIME Reviewed; 585 AA.
AC P18767;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
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=R03283;
GN ORFNames=SMc03900;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN BETA-(1->2)GLUCAN
RP TRANSPORT.
RC STRAIN=102F34;
RX PubMed=3042754; DOI=10.1128/jb.170.8.3523-3530.1988;
RA Stanfield S.W., Ielpi L., O'Brochta D., Helinski D.R., Ditta G.S.;
RT "The ndvA gene product of Rhizobium meliloti is required for beta-
RT (1-->2)glucan production and has homology to the ATP-binding export protein
RT HlyB.";
RL J. Bacteriol. 170:3523-3530(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Involved in beta-(1-->2)glucan export which is required for
CC nodulation of legume roots. May be involved in other classes of
CC oligosaccharides export. Transmembrane domains (TMD) form a pore in the
CC inner membrane and the ATP-binding domain (NBD) is responsible for
CC energy generation (Probable). {ECO:0000305|PubMed:3042754}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA26304.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC47862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M20726; AAA26304.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL591688; CAC47862.1; ALT_INIT; Genomic_DNA.
DR PIR; A31094; VXZRNA.
DR RefSeq; NP_387389.1; NC_003047.1.
DR AlphaFoldDB; P18767; -.
DR SMR; P18767; -.
DR STRING; 266834.SMc03900; -.
DR TCDB; 3.A.1.108.1; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; CAC47862; CAC47862; SMc03900.
DR KEGG; sme:SMc03900; -.
DR PATRIC; fig|266834.11.peg.4842; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_4_5; -.
DR Proteomes; UP000001976; 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 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..585
FT /note="Beta-(1-->2)glucan export ATP-binding/permease
FT protein NdvA"
FT /id="PRO_0000092617"
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 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 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT TRANSMEM 269..289
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 585 AA; 63954 MW; 2B7F115C2A7333F8 CRC64;
MSLFQVYARA LQYLAVHKFR VGAIVIANIV LAAITIAEPI LFGRIIDAIS SQKDVAPMLL
LWAGFGVFNT IAFVLVSREA DRLAHGRRAS LLTEAFGRIV SMPLSWHSQR GTSNALHTLL
RACETLFGLW LEFMRQHLAT AVALMLLIPT AFAMDVRLSL ILVVLGAAYV MISKVVMSRT
KEGQAAVEGH YHTVFSHVSD SISNVSVVHS YNRIEAETRE LKKFTQRLLS AQYPVLDWWA
LASGLNRIAS TISMMAILVI GTVLVQRGEL GVGEVIAFIG FANLLIGRLD QMKAFATQIF
EARAKLEDFF QLEDSVQDRE EPADAGELKG VVGEVEFRDI SFDFANSAQG VRNVSFKAKA
GQTIAIVGPT GAGKTTLVNL LQRVHEPKHG QILIDGVDIA TVTRKSLRRS IATVFQDAGL
MNRSIGENIR LGREDASLDE VMAAAEAAAA SDFIEDRLNG YDTVVGERGN RLSGGERQRV
AIARAILKNA PILVLDEATS ALDVETEARV KDAIDALRKD RTTFIIAHRL STVREADLVI
FMDQGRVVEM GGFHELSQSN GRFAALLRAS GILTDEDVRK SLTAA
