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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
 
 
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