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Database: UniProt
Entry: U1SG64_9BIFI
LinkDB: U1SG64_9BIFI
Original site: U1SG64_9BIFI 
ID   U1SG64_9BIFI            Unreviewed;       376 AA.
AC   U1SG64;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=HMPREF9244_00866 {ECO:0000313|EMBL:ERH30918.1};
OS   Alloscardovia omnicolens F0580.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Alloscardovia.
OX   NCBI_TaxID=1321816 {ECO:0000313|EMBL:ERH30918.1, ECO:0000313|Proteomes:UP000016519};
RN   [1] {ECO:0000313|EMBL:ERH30918.1, ECO:0000313|Proteomes:UP000016519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0580 {ECO:0000313|EMBL:ERH30918.1,
RC   ECO:0000313|Proteomes:UP000016519};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC       apoproteins. Can hydrolyze ATP. {ECO:0000256|HAMAP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERH30918.1}.
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DR   EMBL; AWSI01000021; ERH30918.1; -; Genomic_DNA.
DR   RefSeq; WP_021617998.1; NZ_KE952644.1.
DR   AlphaFoldDB; U1SG64; -.
DR   STRING; 419015.HMPREF3214_00673; -.
DR   PATRIC; fig|1321816.3.peg.768; -.
DR   HOGENOM; CLU_024839_0_0_11; -.
DR   Proteomes; UP000016519; Unassembled WGS sequence.
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   CDD; cd02037; Mrp_NBP35; 1.
DR   Gene3D; 3.30.300.130; Fe-S cluster assembly (FSCA); 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR044304; NUBPL-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR42961; IRON-SULFUR PROTEIN NUBPL; 1.
DR   PANTHER; PTHR42961:SF2; IRON-SULFUR PROTEIN NUBPL; 1.
DR   Pfam; PF01883; FeS_assembly_P; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02040}; 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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02040}; Reference proteome {ECO:0000313|Proteomes:UP000016519}.
FT   DOMAIN          9..77
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   BINDING         125..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   376 AA;  40516 MW;  8E704FBA7A17D89C CRC64;
     MTEERIAREI YARLTGVIDP ELGKSITDLG MVTGVEVDQM EAGHFTVHLH IELTVPHCPL
     SDVIREKIEQ AVASYPDVSL TLDLDVSSMS EEKLNNLVTQ LKQARRENPF HKKGIKTRIF
     AVASGKGGVG KSSVTANLAA AFAAAGYDTA VIDADIYGFS MPRLMGVATH PTNLNGMLMP
     VEAWGTKVMS IGMFAGSDRA ILWRGPRLQR SLEQFLSDVW WGEPDVLLID MAPGTGDMAI
     SVAQALPNAE LIVVTTPQPS ASDIAVRAGL VALQVPMDVA GVVENMSWYE HKGEKLRLFG
     EGGGARVAAQ LSEQLENKLG HRVPLLAQFP LETDIREVGE SGRPAVLNAD GSLACTPLAH
     AFSSMVNSLM ERDYGD
//
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