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Database: UniProt
Entry: A0A1G8VZV5_9GAMM
LinkDB: A0A1G8VZV5_9GAMM
Original site: A0A1G8VZV5_9GAMM 
ID   A0A1G8VZV5_9GAMM        Unreviewed;       370 AA.
AC   A0A1G8VZV5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=SAMN04488540_11242 {ECO:0000313|EMBL:SDJ71387.1};
OS   Ferrimonas sediminum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=718193 {ECO:0000313|EMBL:SDJ71387.1, ECO:0000313|Proteomes:UP000199527};
RN   [1] {ECO:0000313|EMBL:SDJ71387.1, ECO:0000313|Proteomes:UP000199527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23317 {ECO:0000313|EMBL:SDJ71387.1,
RC   ECO:0000313|Proteomes:UP000199527};
RA   de Groot N.N.;
RL   Submitted (OCT-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   -!- 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}.
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DR   EMBL; FNEM01000012; SDJ71387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8VZV5; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000199527; 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; 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          16..85
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   BINDING         116..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   370 AA;  38914 MW;  436D64C2FE259F1B CRC64;
     MNPNPINDQL PEALSAKVLS ILSTQIDPFL NQNLVEAGLV RSLDLDGRCL KLGLVYPYPC
     QSKYRQRVMA LTNALAKLEE IDEVECEIGL SVPQVQAEGQ AEAVKGVKNI VAVSSGKGGV
     GKSTTAVNLA LALASEGARV GLLDADIYGP SVPIMLGVND FQPVSTDGKT MEPAFAHGLA
     AMSIGFMVTE DQATVWRGPM AAGALVQLLN ETNWPDLDYL VIDMPPGTGD IQLTLSQQVP
     VAGAVVVTTP QDIATADARK GITMFNKVNI PVLGIVENMS YHICGQCGSK EHPFGTGGGQ
     ATAERYDVPM LGELPLNVAI REAVDGGNPT VVADPDGDIS AQYKAIAHKT AAALVNLSEP
     TALEIEICDE
//
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