ID   NODI_CUPPJ              Reviewed;         325 AA.
AC   Q46YX6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Nod factor export ATP-binding protein I {ECO:0000255|HAMAP-Rule:MF_01704};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01704};
DE   AltName: Full=Nodulation ATP-binding protein I {ECO:0000255|HAMAP-Rule:MF_01704};
GN   Name=nodI {ECO:0000255|HAMAP-Rule:MF_01704}; OrderedLocusNames=Reut_A2295;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- FUNCTION: Part of the ABC transporter complex NodIJ involved in the
CC       export of the nodulation factors (Nod factors), the bacterial signal
CC       molecules that induce symbiosis and subsequent nodulation induction.
CC       Nod factors are LCO (lipo-chitin oligosaccharide), a modified beta-1,4-
CC       linked N-acetylglucosamine oligosaccharide. This subunit is responsible
CC       for energy coupling to the transport system. {ECO:0000255|HAMAP-
CC       Rule:MF_01704}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (NodI) and
CC       two transmembrane proteins (NodJ). {ECO:0000255|HAMAP-Rule:MF_01704}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01704}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01704}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Lipooligosaccharide exporter (TC 3.A.1.102) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01704}.
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DR   EMBL; CP000090; AAZ61657.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46YX6; -.
DR   SMR; Q46YX6; -.
DR   STRING; 264198.Reut_A2295; -.
DR   EnsemblBacteria; AAZ61657; AAZ61657; Reut_A2295.
DR   KEGG; reu:Reut_A2295; -.
DR   eggNOG; COG1131; Bacteria.
DR   HOGENOM; CLU_000604_1_2_4; -.
DR   OMA; GETVFFY; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR005978; ABC_transptNodI.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01288; nodI; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51240; NODI; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane; Nodulation;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..325
FT                   /note="Nod factor export ATP-binding protein I"
FT                   /id="PRO_0000272602"
FT   DOMAIN          27..257
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
FT   BINDING         59..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
SQ   SEQUENCE   325 AA;  35958 MW;  A5D02C25FFE11EEE CRC64;
     MRGDDRHNGG YCAPPARLPV PALTAILELR KVRKQYGDTV VVNDLDLQVH RGQCFGLLGP
     NGAGKTTTLR LLLGLTTPAG GSLTLCGEPI PERAPQARMR VGVVPQFDNL DPDFSVIENL
     RIFGRYFGLS SAVIERRVPA LLEFARLENR ANAQVRDLSG GMRRRLTVAR ALINDPDLLI
     MDEPTTGLDP QARHLIWERL KSLMASGKTI LLTTHFMEEA ERLCNYLCVI DGGRKIAEGK
     PHDLIDSQIG CDVVEVYGDE LDTLRGSLTP LAERTEMSGE TLFCYVREPA PLLAALHGQS
     GVRYLHRPAN LEDVFLKLTG REMRD