(data stored in ACNUC7421 zone)

SWISSPROT: D6XWR6_BACIE

ID   D6XWR6_BACIE            Unreviewed;       350 AA.
AC   D6XWR6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   OrderedLocusNames=Bsel_0368 {ECO:0000313|EMBL:ADH97908.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97908.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97908.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001791; ADH97908.1; -; Genomic_DNA.
DR   RefSeq; WP_013171337.1; NC_014219.1.
DR   STRING; 439292.Bsel_0368; -.
DR   EnsemblBacteria; ADH97908; ADH97908; Bsel_0368.
DR   KEGG; bse:Bsel_0368; -.
DR   eggNOG; ENOG4105D1F; Bacteria.
DR   eggNOG; COG0489; LUCA.
DR   HOGENOM; HOG000079915; -.
DR   KO; K03593; -.
DR   OMA; PHATAAF; -.
DR   OrthoDB; 1413173at2; -.
DR   BioCyc; BSEL439292:G1GLR-393-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-UniRule.
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_sf.
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; D6XWR6.
DR   SWISS-2DPAGE; D6XWR6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN        4     66       FeS_assembly_P. {ECO:0000259|Pfam:
FT                                PF01883}.
FT   NP_BIND     114    121       ATP. {ECO:0000256|HAMAP-Rule:MF_02040}.
SQ   SEQUENCE   350 AA;  38043 MW;  2D20D0562E997656 CRC64;
     MLTEQQVLDA LKPIKDPHLG VGLLDLDSVK DLKIKENLVS LKLAIAEPGT AEQMQLQQEV
     VNAVKTAGAE SVGLRFEKLP DEVLAEHGGQ SEEAASESLL DRTDRTTFIA VTSGKGGVGK
     STVSVNLATS LARQGKKVGI IDADIYGFSV PDMMGIEERP KVVGQRIYPV TRFDVQVISM
     GFFVEDNSPI IWRGPMLGKM LNNFFSEVEW DDLDYLILDL PPGTGDVALD VHSMLPTSKE
     IVVTTPHATA AFVAARAGAM ALKTDHEILG VVENMAYFES KVTGEKEYVF GTGGGQKLAE
     ELHSEVLAQI PLGQPDFDEE VFAPSVYDQE HPIGKIYMDM AKQVIEKTAK
//

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