(data stored in ACNUC7421 zone)

SWISSPROT: C6B2N3_RHILS

ID   C6B2N3_RHILS            Unreviewed;       388 AA.
AC   C6B2N3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   05-JUL-2017, entry version 52.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   OrderedLocusNames=Rleg_0549 {ECO:0000313|EMBL:ACS54853.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54853.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54853.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54853.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to
CC       target apoproteins. Can hydrolyze ATP. {ECO:0000256|HAMAP-
CC       Rule:MF_02040}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02040}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       {ECO:0000256|HAMAP-Rule:MF_02040}.
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DR   EMBL; CP001622; ACS54853.1; -; Genomic_DNA.
DR   RefSeq; WP_012756235.1; NC_012850.1.
DR   ProteinModelPortal; C6B2N3; -.
DR   EnsemblBacteria; ACS54853; ACS54853; Rleg_0549.
DR   KEGG; rlg:Rleg_0549; -.
DR   HOGENOM; HOG000079914; -.
DR   KO; K03593; -.
DR   OMA; CPNQAIC; -.
DR   OrthoDB; POG091H00OE; -.
DR   BioCyc; RLEG395491:GHX2-549-MONOMER; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02037; MRP-like; 1.
DR   Gene3D; 3.30.300.130; -; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR034904; FSCA_dom.
DR   InterPro; IPR002744; MIP18-like.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   Pfam; PF01883; FeS_assembly_P; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF117916; SSF117916; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B2N3.
DR   SWISS-2DPAGE; C6B2N3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02040}.
FT   DOMAIN        6     75       FeS_assembly_P. {ECO:0000259|Pfam:
FT                                PF01883}.
FT   NP_BIND     137    144       ATP. {ECO:0000256|HAMAP-Rule:MF_02040}.
SQ   SEQUENCE   388 AA;  41032 MW;  AC2436B2CED417B3 CRC64;
     MADVTKEQVL ETLKTVRGPD LEHDIVELGM VSDVFISDGK VYFSITVPAD RAKELEPMRL
     AAERVIKEMP GVKGALVTLT ADKKAAAAAP AARPAANPPH GHAGHDHGSH AHAPQQPPRA
     GKIGVPGIGA IIAVASGKGG VGKSTTAVNL ALGLLANGLR VGILDADIYG PSMPRLLKIS
     GRPTQIDGRI INPMENYGLK VMSMGFLVDE ETAMIWRGPM VQSALLQMLR EVAWGELDVL
     VVDMPPGTGD VQLTMAQQVP LAGAVIVSTP QDLALIDARK GLNMFRKVEV PVLGIVENMS
     YFIAPDTGTR YDIFGHGGAR KEAERIGVPF LGEVPLTMNI RETSDAGTPL VASEPNGVVA
     GIYRGIAAKV WEQVAGQPQR PAPTIVFE
//

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