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NODI_RHILV
ID   NODI_RHILV              Reviewed;         311 AA.
AC   P08720;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 111.
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 leguminosarum bv. viciae.
OG   Plasmid sym pRL1JI.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3019841; DOI=10.1016/0378-1119(86)90012-0;
RA   Evans I.J., Downie J.A.;
RT   "The nodI gene product of Rhizobium leguminosarum is closely related to
RT   ATP-binding bacterial transport proteins; nucleotide sequence analysis of
RT   the nodI and nodJ genes.";
RL   Gene 43:95-101(1986).
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; Y00548; CAA68618.1; -; Genomic_DNA.
DR   PIR; A24400; A24400.
DR   AlphaFoldDB; P08720; -.
DR   SMR; P08720; -.
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..311
FT                   /note="Nod factor export ATP-binding protein I"
FT                   /id="PRO_0000092638"
FT   DOMAIN          13..243
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01704"
SQ   SEQUENCE   311 AA;  34301 MW;  52C2789810648E1A CRC64;
     MDSPSGSLSP VAIDLAGVSK SYGGKIVVND LSFTIAAGEC FGLLGPNGAG KSTITRMILG
     MTSPSVGKIT VLGAQEPGQV RLARAKIGIV SQFDNLDLEF TVRENLLVYG RYFRMSTREI
     ETVIPSLLEF ARLESKANTR VADLSGGMKR RLTLAGALIN DPQLLILDEP TTGLDPHARH
     LIWERLRSLL ARGKTILLTT HIMEEAERLC DRLCVLEAGR KIAEGRPHAL IEEQIGCPVI
     EIYGGDPQEL SLLIRPNARR LEISGETLFC YTPDPEQVRA QLRAYSNLRL LERPPNLEDV
     FLRLTGREME K
 
 
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