ID G2KS65_MICAA Unreviewed; 371 AA.
AC G2KS65;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN OrderedLocusNames=MICA_404 {ECO:0000313|EMBL:AEP08748.1};
OS Micavibrio aeruginosavorus (strain ARL-13).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Micavibrio.
OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP08748.1, ECO:0000313|Proteomes:UP000009286};
RN [1] {ECO:0000313|EMBL:AEP08748.1, ECO:0000313|Proteomes:UP000009286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP08748.1,
RC ECO:0000313|Proteomes:UP000009286};
RX PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA Wang Z., Kadouri D., Wu M.;
RT "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT aeruginosavorus ARL-13.";
RL BMC Genomics 12:453-453(2011).
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}.
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DR EMBL; CP002382; AEP08748.1; -; Genomic_DNA.
DR RefSeq; WP_014101971.1; NC_016026.1.
DR AlphaFoldDB; G2KS65; -.
DR STRING; 856793.MICA_404; -.
DR KEGG; mai:MICA_404; -.
DR eggNOG; COG0489; Bacteria.
DR HOGENOM; CLU_024839_0_0_5; -.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000009286; Chromosome.
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:UP000009286}.
FT DOMAIN 9..78
FT /note="MIP18 family-like"
FT /evidence="ECO:0000259|Pfam:PF01883"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 371 AA; 38985 MW; 7B422A92766F487A CRC64;
MIQKNIPENE ILNALRTVID PATGLDLVGA NRISGLQVRG GDVLFLILID PVQAGAMEAV
RMQAEKTVAA IAGVKKVTAV LTAEREGPAP SMKKGPAPLR EKLPIKHIVA VASGKGGVGK
STVAVNLAVA LAMDGLKVGL MDADIYGPSV PMMLGLQNAP RPVVDADTKK LIPHIAHGVK
AMSMGMLVDA SSPMIWRGPM IQSAIRQFLE DVDWAGSDGE LDVLVVDMPP GTGDAQLTLA
QKVPLSGAVI VSTPQDIALI DARKGIAMFE KVGVKVLGLV ENMSYFCCPG CNTRTDIFGH
GGARDEAAKM NVPLLADIPL QAEIRMLSDA GTPVVSARPG LAEAQSYRAL ARDVMASIAL
ERQDDTRRVT G
//
