NDVA_RHIRD
ID NDVA_RHIRD Reviewed; 588 AA.
AC P0A2V1; P18768;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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};
DE AltName: Full=Attachment protein;
GN Name=ndvA {ECO:0000255|HAMAP-Rule:MF_01728}; Synonyms=chvA;
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BETA-(1->2)GLUCAN TRANSPORT,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=A348;
RX PubMed=2921245; DOI=10.1128/jb.171.3.1609-1615.1989;
RA Cangelosi G.A., Martinetti G., Leigh J.A., Lee C.C., Theines C.,
RA Nester E.W.;
RT "Role of Agrobacterium tumefaciens ChvA protein in export of beta-1,2-
RT glucan.";
RL J. Bacteriol. 171:1609-1615(1989).
RN [2]
RP FUNCTION IN BETA-(1->2)GLUCAN TRANSPORT, AND SUBCELLULAR LOCATION.
RC STRAIN=A348;
RX PubMed=2708321; DOI=10.1128/jb.171.5.2842-2849.1989;
RA Inon de Iannino N., Ugalde R.A.;
RT "Biochemical characterization of avirulent Agrobacterium tumefaciens chvA
RT mutants: synthesis and excretion of beta-(1-2)glucan.";
RL J. Bacteriol. 171:2842-2849(1989).
CC -!- FUNCTION: Involved in beta-(1-->2)glucan export which is required for
CC crown gall tumor formation. Transmembrane domains (TMD) form a pore in
CC the inner membrane and the ATP-binding domain (NBD) is responsible for
CC energy generation (Probable). {ECO:0000305|PubMed:2708321,
CC ECO:0000305|PubMed:2921245}.
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, ECO:0000269|PubMed:2708321, ECO:0000269|PubMed:2921245};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01728,
CC ECO:0000269|PubMed:2708321, ECO:0000269|PubMed:2921245}.
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; M24198; AAA22083.1; -; Genomic_DNA.
DR PIR; A32810; VXAGCA.
DR AlphaFoldDB; P0A2V1; -.
DR SMR; P0A2V1; -.
DR STRING; 1082932.ATCR1_10248; -.
DR PATRIC; fig|358.65.peg.4035; -.
DR eggNOG; COG1132; Bacteria.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Sugar transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..588
FT /note="Beta-(1-->2)glucan export ATP-binding/permease
FT protein NdvA"
FT /id="PRO_0000092232"
FT TRANSMEM 22..42
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 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 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 588 AA; 64651 MW; 667FABF83B4FBEB1 CRC64;
MTLFQVYTRA LRYLTVHKWR VAVVVIANVI LAAITIAEPV LFGRIIDAIS SGTNVTPILI
LWAGFGVFNT VAYVAVAREA DRLAHGRRAT LLTEAFGRII SMPLSWHHLR GTSNALHTLL
RASETLFGLW LEFMRTHLAT FVALVLLIPT AMAMDLRLSF VLIGLGIVYW FIGKWVMGRT
KDGQASVEEH YHSVFAHVSD SISNVSVLHS YNRIEAETKA LKSFTEKLLS AQYPVLDWWA
FASALNRTAS TVSMMIILVI GTVLVKNGEL RVGDVIAFIG FANLLIGRLD QMRQFVTQIF
EARAKLEDFF VLEDAVKERE EPGDARELSN VSGTVEFRNI NFGFANTKQG VHDVSFTAKA
GETVAIVGPT GAGKTTLINL LQRVYDPDSG QILIDGTDIS TVTKNSLRNS IATVFQDAGL
LNRSIRENIR LGRETATDAE VVEAAAAAAA TDFIDSRING YLTQVGERGN RLSGGERQRI
AIARAILKNA PILVLDEATS ALDVETEARV KAAVDALRKN RTTFIIAHRL STVRDADLVL
FLDQGRIIEK GTFDELTQRG GRFTSLLRTS GLLTEDEGQQ PRPKAIAS
