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NDVA_RHILO
ID   NDVA_RHILO              Reviewed;         590 AA.
AC   Q983H5;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
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=mlr8326;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB53906.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q983H5; -.
DR   SMR; Q983H5; -.
DR   STRING; 266835.14027637; -.
DR   EnsemblBacteria; BAB53906; BAB53906; BAB53906.
DR   KEGG; mlo:mlr8326; -.
DR   PATRIC; fig|266835.9.peg.6652; -.
DR   eggNOG; COG1132; Bacteria.
DR   HOGENOM; CLU_000604_84_3_5; -.
DR   OMA; MPVLSWW; -.
DR   Proteomes; UP000000552; 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..590
FT                   /note="Beta-(1-->2)glucan export ATP-binding/permease
FT                   protein NdvA"
FT                   /id="PRO_0000290252"
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        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        275..295
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   590 AA;  64220 MW;  5890063165EAD79B CRC64;
     MSLLQIYWRA LGYLAADKRR VALICGANVA LAAIAILEPI MFGRVIDAIS EHGSVFSTLA
     VWAGLGAFNV IAFVLVARGA DRFAHARRSE VLCQSFERVI TMPLAWHHQR GTSNALHTLL
     RAVETLFSLW LEFMRQHLST AVALVLLVPT ALSMDVRMSM VLLGLGVLYV GIGRLVMKRT
     KAGQAAVERH YHKVFAHVTD SVSNVAVLQS YNRLGHEAET LRRYVKNLLD AQNPVLDWWA
     IANALNRLSS TISMMVVLLI GAYLVTHGQL RVGDVIAFTG FATLLISRLD QMSAFANQIS
     EARAKLEEFY KLEDSAADAA EPDGLRDLTN VTGHVRFEDV GFEFANSGQG VSGVSFEVQA
     GQTVAIVGPT GAGKTTLINL LQRVFSPSTG RILIDGIDTR TVTRKSLRHS IATVFQDAGL
     LNRSIEDNIR VGRADASNVE IHAAAVAAAA QDFILAKSGG YDTVVGERGG QLSGGERQRI
     AIARAVLKDA PILVLDEATS ALDVETEDRV KEAIDELRRD RTTFIIAHRL TTVRDADLVV
     FMDKGRVVEM GGFAELSLRN GRFASLLRAG GLLNDEEVRR LSRSVQGEAA
 
 
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