NODI_NEOGA
ID NODI_NEOGA Reviewed; 347 AA.
AC P50332;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Neorhizobium galegae (Rhizobium galegae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Neorhizobium.
OX NCBI_TaxID=399;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HAMBI 1174;
RX PubMed=10474187; DOI=10.1111/j.1574-6968.1999.tb13735.x;
RA Suominen L., Paulin L., Saano A., Saren A.-M., Tas E., Lindstroem K.;
RT "Identification of nodulation promoter (nod-box) regions of Rhizobium
RT galegae.";
RL FEMS Microbiol. Lett. 177:217-223(1999).
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; X87578; CAA60881.1; -; Genomic_DNA.
DR AlphaFoldDB; P50332; -.
DR SMR; P50332; -.
DR TCDB; 3.A.1.102.1; the atp-binding cassette (abc) superfamily.
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..347
FT /note="Nod factor export ATP-binding protein I"
FT /id="PRO_0000092637"
FT DOMAIN 49..279
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
SQ SEQUENCE 347 AA; 38436 MW; AC791210C44C9A6C CRC64;
MGENMEREML RPKTIAMDQN SASARSNPER EIKTGRLEPA SNSAPTMAID LQAVTMIYRD
KTVVDSLSFG VRAGECFGLL GPNGAGKSTI TRMLLGMATP SAGKISVLGL PVPGKARLAR
ASIGVVSQFD NLDMEFTVRE NLLVFGRYFQ MSTRAIEKLI PSLLEFAQLE AKADVRVSDL
SGGMKRRLTL ARALVNDPQL LILDEPTTGL DPPARHQIWE RLRSLLIRGK TILLTTHMMD
EAERMCDRLC VLEGGRMIAE GPPLSLIEDI IGCPVIEVYG GNPDELSLIV RPHVDRIETS
GETLFCYTVN SDQVRAKLRE FPSLRLLERP ANLEDVFLRL TGREMEK