NDVA_RHOP5
ID NDVA_RHOP5 Reviewed; 602 AA.
AC Q07QX6;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=RPE_1709;
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC Rule:MF_01728}.
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}.
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DR EMBL; CP000463; ABJ05658.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07QX6; -.
DR SMR; Q07QX6; -.
DR STRING; 316055.RPE_1709; -.
DR EnsemblBacteria; ABJ05658; ABJ05658; RPE_1709.
DR KEGG; rpe:RPE_1709; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_1_5; -.
DR OMA; MPVLSWW; -.
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; 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 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..602
FT /note="Beta-(1-->2)glucan export ATP-binding/permease
FT protein NdvA"
FT /id="PRO_0000290253"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT DOMAIN 21..311
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT DOMAIN 345..579
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT BINDING 378..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
SQ SEQUENCE 602 AA; 65944 MW; D57760C14851C6A8 CRC64;
MPMLRLYARV LQLLGKEAML GWVLAGANLL LAAAQFAEPV LFGRIVDVLS GNLSTGAMAQ
PAQSPWPLLL AWAVFGLFTI GCGAAVALHA DRLAHRQRQA ILTDYFEHVL QLPLTYHTGT
HSGRLMKVML NGTDALWRLW LGFFREHFAA LMSLVVLLPL SIYINWRLAL LLFALCVVFT
VLTTLVVRKT YAMQGEVEES YSDLSARASD ALGNIALVQS FVRIDAEVQG LRFVADRLLA
MQMPVLSWWA LVTVITRAST TITVLAIFTV GIALHEQGLT SVGEIVMFVS FATMLIQKLE
QVVGFVNSVF MEAPRLQEFV NVLDAVPAVR DRLDAIDPGR LSGLVEFDNV SFSYDGKRPA
IEDLSFTALP GQTIALVGAT GAGKSTAIAL LHRAFDPQSG VIKIDGMDVR GLTLAGLRRN
IGVVFQEALL FDRTIADNLR VGKPDATEEE MRIAASRAQA LDFIERSELK FDTNAGERGR
MLSGGERQRL SIARALLKDP PILILDEATS ALDAVTEAKV NLALDEVMKG RTTFVIAHRL
STIRHATRIL VFDNGRVIES GSFDELLARR GYFAELAHAQ FMVQDSARSA MPAAQPEGIP
EF