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NDVA_BARQU
ID   NDVA_BARQU              Reviewed;         595 AA.
AC   Q6FZF2;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=BQ07930;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF26276.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6FZF2; -.
DR   SMR; Q6FZF2; -.
DR   STRING; 283165.BQ07930; -.
DR   EnsemblBacteria; CAF26276; CAF26276; BQ07930.
DR   KEGG; bqu:BQ07930; -.
DR   eggNOG; COG1132; Bacteria.
DR   HOGENOM; CLU_000604_84_8_5; -.
DR   OMA; MPVLSWW; -.
DR   OrthoDB; 643917at2; -.
DR   Proteomes; UP000000597; 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   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_0000290242"
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        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        152..172
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   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;  66351 MW;  BFCFE470AC67A70D CRC64;
     MSLFKAYARV LTYLKKEKNT SLLICAANVM LAIITIAEPI LFGRVIDSIA EKSAIILTLT
     IWVCFGISHI IAYVLVARSA DRLTHRHRLA VLTESFERII AMPLSWHQQR GTSNALHILL
     RAIDSMSAIW LDFMRQHLST LVALFILIPI AFNMNWRLSI VLVVLAIIYV LIARLVMRKT
     KDGQAAVECY HHNLFQHVSD SISNVSIVQS YNRIREETSA LHNYTNDLLK AQNPVLNWWA
     LASGLNRTAS TISIVCVLLL GAFFVAKGQL RVGEVVAFVG FAQLMISRLD QMSNFINLTV
     SSQAKLQEFF SMEDSTFHIN EPENLPCLQN VKGTVQFHHV TYKFPNSSQG VFDISFKVKT
     GQTVAIVGPT GAGKTTLINL LQRVYEPTFG HISIDGINIR SINRESLRKS LATVFQDAGL
     FNRSIHDNIL IGRATATNEE LYEAAKIAAA HDFILKKTDR YNTMVGERGS QLSGGEKQRL
     AIARAVLKNA PILILDEATS ALDVETEARV KDALDCISHN RTTFIIAHRL STVRHADLVL
     FLENGHLIEK GNFQELIDKG GRFYKLLKAG GLIIDQPTIK GEDKNVIPLR EAIAS
 
 
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