ID   NDVA_BARBA              Reviewed;         595 AA.
AC   P70864;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
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};
OS   Bartonella bacilliformis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Upeslacis E., Ihler G.M.;
RL   Submitted (AUG-1996) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB09036.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U68242; AAB09036.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P70864; -.
DR   SMR; P70864; -.
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   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..595
FT                   /note="Beta-(1-->2)glucan export ATP-binding/permease
FT                   protein NdvA"
FT                   /id="PRO_0000290239"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        129..149
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        252..272
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   595 AA;  66245 MW;  8C642CAED6D04E49 CRC64;
     MSLFRTYVRV LSYLNQEKNA FLLICTANIT LAIITIAEPI LFGHVIDTIA DKSDTLVTLA
     VWMCFGISNI IAYVLVARGA DRLAHRCRLT VLEKSFARII SMPLIWHQQR GTSHALHTLL
     RATDSMSSIW LEFMRQHLST FVALFVLVPV TFKMNWRLSI VLMVLAILYI LIARLVMQKT
     KNGQAAVEHY HHNLFKHITD SISNVSIVQS YNRITEETSA LHQHTNNLLS AQTPVLNWWA
     LASGLNRMAS TISIVCVLLL GAFFVIKGQL SVGEVVTFVG FSQLMIGRLD QISGFINLAV
     SSQAKLQEFF DMEDSTFQTN EPANLPSLPN VKGAIQFHHV TYEFPNSSQG VFDISFEVKA
     GQTVAIVGPT GAGKTTLINL LQRVYDPTVG YISIDGININ SINRESLRKA LATVFQDAGL
     FDRTIRDNIS IGKTGATDEE LYEATKTASA HDFILKKSKN YDTLVGERGS QLSGGERQRL
     AIARAILKNA PILILDEATS ALDVETEIRV KNAIDCISQN RTTFIIAHRL STIRNADLVL
     FLDQGRLIEK GSFQELINKD GHFYKLLKRG GLTINQPATK EKDDNIIPLR KAMAL