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Database: UniProt
Entry: A0A080N4F4_9BIFI
LinkDB: A0A080N4F4_9BIFI
Original site: A0A080N4F4_9BIFI 
ID   A0A080N4F4_9BIFI        Unreviewed;       381 AA.
AC   A0A080N4F4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=BBOMB_0650 {ECO:0000313|EMBL:KFF31305.1};
OS   Bifidobacterium bombi DSM 19703.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF31305.1, ECO:0000313|Proteomes:UP000028730};
RN   [1] {ECO:0000313|EMBL:KFF31305.1, ECO:0000313|Proteomes:UP000028730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF31305.1,
RC   ECO:0000313|Proteomes:UP000028730};
RX   PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA   Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA   Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA   Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT   "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL   Appl. Environ. Microbiol. 80:6290-6302(2014).
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:KFF31305.1}.
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DR   EMBL; ATLK01000001; KFF31305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A080N4F4; -.
DR   STRING; 1341695.BBOMB_0650; -.
DR   eggNOG; COG0489; Bacteria.
DR   Proteomes; UP000028730; 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}; Reference proteome {ECO:0000313|Proteomes:UP000028730}.
FT   DOMAIN          16..93
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   BINDING         139..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   381 AA;  40311 MW;  C8AAFC2236F24BC5 CRC64;
     MPGQENMTDV TVIRGNVYER LSHVIDPEIG RSVTDLGMIV AIDVAPSHST EGVRAPGRFD
     VTVHVELTVP GCPLTQTIQD RIDEAVASYP GLELVPHIEV GAMDADKLTG LVSSLKAERR
     ENPFNKPGIK TRIFAIASGK GGVGKSSVSA NLAATFSALG YDTAAIDADI YGFSLPGLFG
     VHSQPTNLNG MLMPVTAWGV KLISIGMFAG ADRAILWRGP RLQRSLEQFL SDVWWGQPDV
     LLLDLAPGTG DMAISVAQAL PNAELVVVTT PQPSASDVAV RSGLVALQVP LKVRGVVENM
     SYFDHAGERL RIFGEGGGTR VSDRLTDALG YDVPLLASLP LEPDIREVGE SGRPAVLDSD
     GSLADTPLAS SFTALARRLI G
//
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