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
//