NDVA_RHOP2
ID NDVA_RHOP2 Reviewed; 602 AA.
AC Q2J0F4;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-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}; OrderedLocusNames=RPB_1346;
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-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 (By similarity).
CC {ECO:0000250}.
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; CP000250; ABD06056.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2J0F4; -.
DR SMR; Q2J0F4; -.
DR STRING; 316058.RPB_1346; -.
DR EnsemblBacteria; ABD06056; ABD06056; RPB_1346.
DR KEGG; rpb:RPB_1346; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_8_5; -.
DR OMA; MPVLSWW; -.
DR Proteomes; UP000008809; 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; 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_5000107147"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT TRANSMEM 66..86
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 254..274
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..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; 65798 MW; 75713D927115EE6C CRC64;
MSLFRVYTRV LELLGKERRL GWTLAVANLL LATAQFAEPV LFGRIVDVMS GNLATGALAP
EARSPWPLLA AWVGFGLFTI FCSAAVSLHA DRLAHRQRQA VLTSYFEHIL QLPTTFHTGT
HSGRLIKVML QGTDALWRVW LGFFREHFAA LLSLLVLLPL SLYINWRLAM LLFALCGVFT
VLTTLVVRKT YGLQSEVEAQ YSDLSARASD ALGNVALVQS YVRIDAEVQG LRFVADKLLA
AQMPVLSWWA LVTVITRAST TITVLAIFAL GIVLNQQGLT SIGEIVMFVS FATLLIQRLE
QVVSFVNSLM MEAPRLQEFI DVLDEVPAVR DRPNAIDPGR LSGLVEFQDV SFSYDGKRPA
VEDLSFTALP GQTIALVGAT GAGKSTAIAL LHRAFDPQSG TVKIDGMDIR GLTLAGLRRN
IGVVFQEALL FDRSIADNLR VGKPDATDAE LRLAAERAQA LDFIERSGLG FNTAAGERGR
MLSGGERQRL SIARALLKDP PILILDEATS ALDAVTEAKV NLALDEVMRG RTTFVIAHRL
STIRHATRIL VFENGRVIES GTFDDLVAQR GHFAELARAQ FMVQEDARAS VAAAADHASV
RP
