ID   APBC_METMP              Reviewed;         289 AA.
AC   Q6LZC5;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040, ECO:0000303|PubMed:19114487};
GN   OrderedLocusNames=MMP0704 {ECO:0000312|EMBL:CAF30260.1};
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF CYS-218 AND CYS-221.
RC   STRAIN=S900;
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       ECO:0000269|PubMed:19114487}.
CC   -!- DOMAIN: The N-terminal cysteine-rich ferredoxin-like domain is not
CC       required for activity. {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; BX950229; CAF30260.1; -; Genomic_DNA.
DR   RefSeq; WP_011170648.1; NC_005791.1.
DR   AlphaFoldDB; Q6LZC5; -.
DR   SMR; Q6LZC5; -.
DR   STRING; 267377.MMP0704; -.
DR   PRIDE; Q6LZC5; -.
DR   EnsemblBacteria; CAF30260; CAF30260; MMP0704.
DR   GeneID; 37875235; -.
DR   KEGG; mmp:MMP0704; -.
DR   PATRIC; fig|267377.15.peg.721; -.
DR   eggNOG; arCOG00585; Archaea.
DR   HOGENOM; CLU_024839_0_1_2; -.
DR   OMA; NMAYFTP; -.
DR   OrthoDB; 32313at2157; -.
DR   BioCyc; MMAR267377:MMP_RS03685-MON; -.
DR   Proteomes; UP000000590; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR23264; PTHR23264; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..289
FT                   /note="Iron-sulfur cluster carrier protein"
FT                   /id="PRO_0000433953"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
FT   MUTAGEN         218
FT                   /note="C->A: Decrease in activity. Lack of activity; when
FT                   associated with A-221."
FT                   /evidence="ECO:0000269|PubMed:19114487"
FT   MUTAGEN         221
FT                   /note="C->A: Decrease in activity. Lack of activity; when
FT                   associated with A-218."
FT                   /evidence="ECO:0000269|PubMed:19114487"
SQ   SEQUENCE   289 AA;  31034 MW;  CDCBE95B03EC4A8D CRC64;
     MAEECSGNCD SCGSSSDCSD TKKMMEQQNA QIRDNMSKIK YKIAVMSGKG GVGKSTVTVN
     LAATLNMMGY KVGVLDGDIH GPNIPQMLGV DQIQPMADEN GIYPVSTPQG IKTMSIGYFL
     PDKNTPIIWR GPKASGAIRQ FLSDVNWGEL DFLLIDTPPG SGDIQITTLQ AIPDIDGVVI
     VTTPEEVSVL DARKSVSAAN TLEIPIIGIV ENMGGFVCPE CDKVIDIFGK GGGEKAAKEL
     NVFFLGRIPL DIKARVASDR GVPMVTMDCK ASEEFKKVVN TVLERIKKE