NODI_RHIS3
ID NODI_RHIS3 Reviewed; 304 AA.
AC P72335;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
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};
OS Rhizobium sp. (strain N33).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=103798;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8755627; DOI=10.1094/mpmi-9-0523;
RA Cloutier J., Laberge S., Prevost D., Antoun H.;
RT "Sequence and mutational analysis of the common nodBCIJ region of Rhizobium
RT sp. (Oxytropis arctobia) strain N33, a nitrogen-fixing microsymbiont of
RT both arctic and temperate legumes.";
RL Mol. Plant Microbe Interact. 9:523-531(1996).
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; U53327; AAB16898.1; -; Genomic_DNA.
DR AlphaFoldDB; P72335; -.
DR SMR; P72335; -.
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..304
FT /note="Nod factor export ATP-binding protein I"
FT /id="PRO_0000092644"
FT DOMAIN 6..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
SQ SEQUENCE 304 AA; 33698 MW; 7C6A33B0364CCE14 CRC64;
MSKVAIDLAG VKKSFGDKLV VNGLSFTVAS GECFGLLGPN GAGKSTIARM LLGMTVPDAG
KITVLGEPVG ARSRLARKSI GVVPQFDNLD QEFTVRENLL VFGRYFGMST RKIKEVIPSL
LEFARLESKA DARVGELSGG MKRRLTLARA LINDPQLLVM DEPTTGLDPH ARHLIWERLR
FLLARGKTII LTTHFMEEAE RLCDRLCVLE HGRKLAEGSP HALIEEHIGC QVIEIFGGNP
QELVSLIRPY VQRVEVSGET LFCYTADPEQ VRVQLRGRAG LRLLERPPSL EDVFLRLTGR
EMEK
