NODI_RHIML
ID NODI_RHIML Reviewed; 335 AA.
AC Q8GNH6;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OG Plasmid megaplasmid.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=382;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=102L4;
RX PubMed=12455608; DOI=10.1139/w02-072;
RA Barran L.R., Bromfield E.S., Brown D.C.;
RT "Identification and cloning of the bacterial nodulation specificity gene in
RT the Sinorhizobium meliloti-Medicago laciniata symbiosis.";
RL Can. J. Microbiol. 48:765-771(2002).
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; AF522456; AAN62904.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GNH6; -.
DR SMR; Q8GNH6; -.
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; Plasmid; Translocase; Transport.
FT CHAIN 1..335
FT /note="Nod factor export ATP-binding protein I"
FT /id="PRO_0000092642"
FT DOMAIN 37..267
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
SQ SEQUENCE 335 AA; 36879 MW; 8826A6330FD63CC6 CRC64;
MTQEVPRRLE PSPFEWKGDA GPSVKTLRPH AIPSVAIDLA SVTKSYGDKP VVDGLSFTVA
AGECFGLLGP NGAGKSTITR MILGMTTPAT GVITVLGVPV PSRARLARMG IGVVPQFDNL
DSEFTVRENL LVFGRYFRMS TREIEAVIPS LLEFARLENK VDARVSDLSG GMKRRLTLAR
ALINDPQLLI LDEPTTGLDP HARHLIWERL RSLLARGKTI LLTTHIMEEA ERLCDRLCVL
EAGRKIAEGR PHVLIDEKIG CQVIEIYGGN PHELSALVSP HARHVEVSGE TVFCYALDPE
QVRVQLDGCA GVRFLQRPPN LEDVFLRLTG RELKD
