NODI_BURTA
ID NODI_BURTA Reviewed; 304 AA.
AC Q2SVP3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
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}; OrderedLocusNames=BTH_I2485;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC36763.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000086; ABC36763.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_009891327.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SVP3; -.
DR SMR; Q2SVP3; -.
DR PRIDE; Q2SVP3; -.
DR EnsemblBacteria; ABC36763; ABC36763; BTH_I2485.
DR KEGG; bte:BTH_I2485; -.
DR HOGENOM; CLU_000604_1_2_4; -.
DR Proteomes; UP000001930; Chromosome I.
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_0000272600"
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; 33864 MW; 3CC7967317740B7B CRC64;
MSVAPIDFQQ VEKRYDDKLV VDGLSFHVQP GECFGLLGPN GAGKTTALKM LLGITHPDAG
SISLCGEPVP SRARHARRRV GVVPQFDNLD PDFTVRENLL VFARYFGLAA HEARALVPPL
LEFAKLENKA DAKVGELSGG MKRRLTLARA LVNNPDVLVL DEPTTGLDPQ ARHLMWERLR
SLLVRGKTIL LTTHFMEEAE RLCHRLCVIE EGRKIAEGAP RTLIESEIGC DVIEIYGPDP
AQLREELAPF AERTEISGET LFCYVDDPEP VNARLKGRAG LRYLHRPANL EDVFLRLTGR
EMQD