APBC_PYRAB
ID APBC_PYRAB Reviewed; 295 AA.
AC Q9V0D9; G8ZH61;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN OrderedLocusNames=PYRAB08510; ORFNames=PAB1795;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC {ECO:0000255|HAMAP-Rule:MF_02040}.
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DR EMBL; AJ248285; CAB49765.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70256.1; -; Genomic_DNA.
DR PIR; D75131; D75131.
DR RefSeq; WP_010867974.1; NC_000868.1.
DR AlphaFoldDB; Q9V0D9; -.
DR SMR; Q9V0D9; -.
DR STRING; 272844.PAB1795; -.
DR EnsemblBacteria; CAB49765; CAB49765; PAB1795.
DR GeneID; 1496200; -.
DR KEGG; pab:PAB1795; -.
DR PATRIC; fig|272844.11.peg.900; -.
DR eggNOG; arCOG00585; Archaea.
DR HOGENOM; CLU_024839_0_1_2; -.
DR OMA; NMAYFTP; -.
DR OrthoDB; 32313at2157; -.
DR PhylomeDB; Q9V0D9; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
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; IPR044304; NUBPL-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR42961; PTHR42961; 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.
FT CHAIN 1..295
FT /note="Iron-sulfur cluster carrier protein"
FT /id="PRO_0000184954"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ SEQUENCE 295 AA; 32035 MW; CA719380E1716E45 CRC64;
MTIKAPALNL PGLGADPLTQ RIKEKEKKWK YKVAVLSGKG GVGKSTVAVN LTAALAKMGY
FVGILDADIH GPNVAKMLGV EKEEIYAEKF DDGHFEMIPP MADFMGQVTP IKVMSMGMMV
PEDQPIIWRG ALVTKAIKQL LGDVKWGSLD FMIIDFPPGT GDEILTVVQS IQLDAAIIVT
TPQEVALLDT GKAVNMMKKM EVPYIAVVEN MSYLICPHCG NKIDIFGEGG GEKLAEKEGV
DFLGKIPIDL KAREASDLGI PIVLYGDTPA AKAFMEIAEK LVNKLKEMKG DEKKE
