ID A0A2N6UZ73_9ACTO Unreviewed; 362 AA.
AC A0A2N6UZ73;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=CJ184_02785 {ECO:0000313|EMBL:PMC90312.1};
OS Actinotignum urinale.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinotignum.
OX NCBI_TaxID=190146 {ECO:0000313|EMBL:PMC90312.1};
RN [1] {ECO:0000313|EMBL:PMC90312.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0759 {ECO:0000313|EMBL:PMC90312.1};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) 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 -!- SIMILARITY: In the C-terminal section; belongs to the Mrp/NBP35 ATP-
CC binding proteins family. {ECO:0000256|ARBA:ARBA00008205}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MIP18 family.
CC {ECO:0000256|ARBA:ARBA00007352}.
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:PMC90312.1}.
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DR EMBL; PNHX01000003; PMC90312.1; -; Genomic_DNA.
DR RefSeq; WP_022866618.1; NZ_CP126967.1.
DR AlphaFoldDB; A0A2N6UZ73; -.
DR STRING; 1120933.GCA_000420445_01144; -.
DR OrthoDB; 9809679at2; -.
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; 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; 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.
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 5..70
FT /note="MIP18 family-like"
FT /evidence="ECO:0000259|Pfam:PF01883"
FT BINDING 118..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 362 AA; 39488 MW; 38F2277D3585FBC7 CRC64;
MVTREHILKA LSSIIDPELR HPITELDMVH RVTITDTGKV EVTILLTTAR CPRSEEIERE
VREKIESLGV TDVHVTMGVM TGLQIQKLQE KLKAGRATRN IPFAKENSPT YVIAIASGKG
GVGKSTVAAN LAVTLAKKGA SVGLIDADIY GFSIPSMLGV DTPAQQLNGM IIPPVAHGIK
IMSIGMFVPD GSPVVWRGPM LHKALEQFFA DVYWGDLDFI ILDLPPGTGD VTISISQLLP
YAHILVVTTP QTAAADVALR AGSVSKQTEQ KTVGVVENMS YMEMPDGTRN YIFGKDGGKN
IARKLTKNLG YDIPLLAQIP FETDIREGGD VGEPFTLDIR TSRARKEFEQ LADYFMKTRQ
TS
//
