ID A0A0S8EU92_9BACT Unreviewed; 389 AA.
AC A0A0S8EU92;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=AMK72_00685 {ECO:0000313|EMBL:KPK51037.1};
OS Planctomycetes bacterium SM23_25.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704028 {ECO:0000313|EMBL:KPK51037.1, ECO:0000313|Proteomes:UP000052058};
RN [1] {ECO:0000313|EMBL:KPK51037.1, ECO:0000313|Proteomes:UP000052058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_25 {ECO:0000313|EMBL:KPK51037.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK51037.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJTY01000005; KPK51037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EU92; -.
DR PATRIC; fig|1704028.3.peg.1326; -.
DR Proteomes; UP000052058; 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 CDD; cd00851; MTH1175; 1.
DR Gene3D; 3.30.420.130; Dinitrogenase iron-molybdenum cofactor biosynthesis domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR InterPro; IPR003731; Di-Nase_FeMo-co_biosynth.
DR InterPro; IPR036105; DiNase_FeMo-co_biosyn_sf.
DR InterPro; IPR000808; Mrp-like_CS.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR033913; MTH1175_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR NCBIfam; NF041136; MrpORP; 1.
DR PANTHER; PTHR23264:SF19; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP1; 1.
DR PANTHER; PTHR23264; NUCLEOTIDE-BINDING PROTEIN NBP35 YEAST -RELATED; 1.
DR Pfam; PF02579; Nitro_FeMo-Co; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF53146; Nitrogenase accessory factor-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01215; MRP; 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 286..376
FT /note="Dinitrogenase iron-molybdenum cofactor biosynthesis"
FT /evidence="ECO:0000259|Pfam:PF02579"
FT BINDING 19..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 389 AA; 40786 MW; 5BC5568B922CED29 CRC64;
MALRRRMAEI RCKILVLSGK GGVGKSTVAA NLAMSLALAG KKVGLLDVDL HGPSIPKILG
LEDQRLGPDA AGGIAPIHIT EGLSVVSIGL LLDSAKDAVI WRGPLKYNVI RQFLKDVAWG
KLDYLVVDSP PGTGDEPLSV AQMVGNGAMA VLVTTPQEVA VSDVRRCVSF CKSLSLRVAG
IVENMSGLVC PHCGGQIDLF KAGGGRKLAE EMGVPFLGAI PLDPQIVVSG DSGRAFVQHD
RQSSAAKAFA AAVAPIVNQG RPDAALSSVE GSKEKSRMKI AIPTADGRLA AHFGHCEQFA
LVEVDQDSKT ISRVDYLPPP PHEPGVLPRW LHEQGADLVI AGGMGRRAQG LFRENGMQVV
VGAPADTPES IVTAYLSGTL EAGQNVCDH
//
