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Database: UniProt
Entry: A0A176U3A9_9FIRM
LinkDB: A0A176U3A9_9FIRM
Original site: A0A176U3A9_9FIRM 
ID   A0A176U3A9_9FIRM        Unreviewed;       248 AA.
AC   A0A176U3A9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=HMPREF2738_02938 {ECO:0000313|EMBL:OAD87136.1};
OS   Clostridiales bacterium KLE1615.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1715004 {ECO:0000313|EMBL:OAD87136.1, ECO:0000313|Proteomes:UP000077212};
RN   [1] {ECO:0000313|EMBL:OAD87136.1, ECO:0000313|Proteomes:UP000077212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1615 {ECO:0000313|EMBL:OAD87136.1,
RC   ECO:0000313|Proteomes:UP000077212};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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:OAD87136.1}.
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DR   EMBL; LXPQ01000220; OAD87136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176U3A9; -.
DR   PATRIC; fig|1715004.3.peg.2929; -.
DR   Proteomes; UP000077212; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
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; PF10609; ParA; 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:UP000077212}.
FT   BINDING         20..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   248 AA;  26613 MW;  C391CCD6E2B3559D CRC64;
     MQVKENAHSR VKKVIGVVSG KGGVGKSMVT SLLAVAMNRK GYKTAIMDAD ITGPSIPTAF
     GLNDHAVAND DGLLPEVTKN GIKVMSLNLL LEDQTDPVVW RGPIISGTVS QFWTEVCWGD
     VDYMFVDMPP GTGDVALTVF QSLPLAGIVI VTSPQELVSM IVTKAVKMAE MMNVPVLGIV
     ENMSYFVCPD CGKKHFLFGT SHIEKVAAEH GISVIDYLPL DPKMAALCDE GKMEEAPEGL
     LEKMSSSL
//
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