ID A0A374AFQ6_9BACT Unreviewed; 350 AA.
AC A0A374AFQ6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=DWW03_04425 {ECO:0000313|EMBL:RGH19693.1};
OS Alistipes sp. AF14-19.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=2292910 {ECO:0000313|EMBL:RGH19693.1, ECO:0000313|Proteomes:UP000263263};
RN [1] {ECO:0000313|EMBL:RGH19693.1, ECO:0000313|Proteomes:UP000263263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF14-19 {ECO:0000313|EMBL:RGH19693.1,
RC ECO:0000313|Proteomes:UP000263263};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RGH19693.1}.
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DR EMBL; QTXM01000003; RGH19693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374AFQ6; -.
DR Proteomes; UP000263263; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02040};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02040}.
FT DOMAIN 2..71
FT /note="MIP18 family-like"
FT /evidence="ECO:0000259|Pfam:PF01883"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 350 AA; 37372 MW; 026C2F700E83E45E CRC64;
MEEKIKRLLA SVVHPETGQD IVSSGFIEHT ASAEGKVTVV LRFAKARDPF AVKIKNQAES
LLREAFPGAE VLVVIKEGGA APRPEPKLKT TTGGIARVIA VASGKGGVGK STVTANLAIA
LRNMGFRVGV LDADIYGPSQ PKMFGVEGYM PEAVAEDGVD HIVPAESMDV KLMSIGFFIK
PTDALLWRGA MAVSALKQMI HQTRWGTLDF LLTDLPPGTG DVHLSIIGEL KIDAAVIVST
PQQIAVADVV RGVEMFRNEN VNIPVAGIVE NMAWFTPAEL PENRYYIFGR GGARAYAEKS
GVEFLGEIPI IQSIMDGADA GTPAAGIDSR VEEHYRGIAE KIVGKVMKNG
//
