APBC_SACS2
ID APBC_SACS2 Reviewed; 296 AA.
AC Q97ZW4;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040, ECO:0000303|PubMed:19114487};
GN OrderedLocusNames=SSO0460 {ECO:0000312|EMBL:AAK40784.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=19114487; DOI=10.1128/jb.01469-08;
RA Boyd J.M., Drevland R.M., Downs D.M., Graham D.E.;
RT "Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier
RT proteins.";
RL J. Bacteriol. 191:1490-1497(2009).
CC -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040,
CC ECO:0000269|PubMed:19114487}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC -!- MISCELLANEOUS: Although the second Cys residue of the CXXC motif is
CC replaced with Asp, the protein has Fe-S carrier activity, suggesting
CC that individual cysteine residues in the CXXC motif are dispensable for
CC Fe-S cluster binding. {ECO:0000269|PubMed:19114487}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC {ECO:0000255|HAMAP-Rule:MF_02040}.
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DR EMBL; AE006641; AAK40784.1; -; Genomic_DNA.
DR PIR; A90191; A90191.
DR RefSeq; WP_010922978.1; NC_002754.1.
DR AlphaFoldDB; Q97ZW4; -.
DR SMR; Q97ZW4; -.
DR STRING; 273057.SSO0460; -.
DR EnsemblBacteria; AAK40784; AAK40784; SSO0460.
DR GeneID; 7814131; -.
DR GeneID; 7940321; -.
DR GeneID; 8761734; -.
DR KEGG; sso:SSO0460; -.
DR PATRIC; fig|273057.12.peg.454; -.
DR eggNOG; arCOG00585; Archaea.
DR HOGENOM; CLU_024839_0_1_2; -.
DR InParanoid; Q97ZW4; -.
DR OMA; NMAYFTP; -.
DR PhylomeDB; Q97ZW4; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264; PTHR23264; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..296
FT /note="Iron-sulfur cluster carrier protein"
FT /id="PRO_0000433954"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ SEQUENCE 296 AA; 32048 MW; 20732413716BB566 CRC64;
MSSNPFRIQN PQPQPQRQPR DLRKVNQQVQ AVDLKVQMKM KNIKYKIGVV SGKGGVGKSF
VSSNLAMAIA ASGRKVGIVD VDFHGPSVPK MLGVRGQMLT ADDKGINPVI GPFGIKVVSI
DFLLPRDDTP VVWRGAIKHS AIKQFLGDVN WGELDYLIID MPPGTGDEAL SIAQLVPGIT
GFVIVTIPSE VSTLAVKKSI NFARTVNTKI LGVVENMSHF VCPSDGKVYY IFGEGKGKKM
AEEMGVDLLG QVPLDPSIAE ANDAGEPFFL KHPDSPTSKE FLNIADKVIK IVESNQ