ID B7CAN1_9FIRM Unreviewed; 277 AA.
AC B7CAN1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=EUBIFOR_01252 {ECO:0000313|EMBL:EEC90212.1};
OS Holdemanella biformis DSM 3989.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Holdemanella.
OX NCBI_TaxID=518637 {ECO:0000313|EMBL:EEC90212.1, ECO:0000313|Proteomes:UP000004315};
RN [1] {ECO:0000313|EMBL:EEC90212.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC90212.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEC90212.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC90212.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium biforme (DSM 3989).";
RL Submitted (NOV-2008) 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:EEC90212.1}.
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DR EMBL; ABYT01000068; EEC90212.1; -; Genomic_DNA.
DR RefSeq; WP_003865044.1; NZ_DS996842.1.
DR AlphaFoldDB; B7CAN1; -.
DR STRING; 518637.EUBIFOR_01252; -.
DR eggNOG; COG0489; Bacteria.
DR HOGENOM; CLU_024839_0_2_9; -.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000004315; 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; IPR000808; Mrp-like_CS.
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.
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 BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 277 AA; 30279 MW; 06582E9B3D66B414 CRC64;
MSCEGCPSQG KCGKSSETCG IQSNPDNHIK NIITVMSGKG GVGKSTVTVM LAKAMAKKGL
KVGIMDADIT GPSIPRLLAL SNQHAFGNEK QQLIPVESKE GIKVMSLNFL VQSESDPVIW
RGPVIGGVVK QFYTDVVWGD LDVLLIDMPP GTGDVALTIM QSIPVQGVVM VSTPQPMVSM
IVEKACHMCE KMEVKVLGII ENMAYLECPN CHERIEFYKK EDVETLCNST CTKLYGTLPM
LDLIRDINEY DAYSKDQQEK VDAYLNDIAN EILEDIA
//
