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Database: UniProt
Entry: A0A2S0VVT9_9ALTE
LinkDB: A0A2S0VVT9_9ALTE
Original site: A0A2S0VVT9_9ALTE 
ID   A0A2S0VVT9_9ALTE        Unreviewed;       364 AA.
AC   A0A2S0VVT9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=C2869_18795 {ECO:0000313|EMBL:AWB68329.1};
OS   Saccharobesus litoralis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Saccharobesus.
OX   NCBI_TaxID=2172099 {ECO:0000313|EMBL:AWB68329.1, ECO:0000313|Proteomes:UP000244441};
RN   [1] {ECO:0000313|EMBL:AWB68329.1, ECO:0000313|Proteomes:UP000244441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB-QB4 {ECO:0000313|EMBL:AWB68329.1,
RC   ECO:0000313|Proteomes:UP000244441};
RA   Tan W.R., Lau N.-S., Go F., Amirul A.-A.A.;
RT   "Genome sequence of a Cantenovulum-like bacteria.";
RL   Submitted (JAN-2018) 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}.
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DR   EMBL; CP026604; AWB68329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0VVT9; -.
DR   KEGG; cate:C2869_18795; -.
DR   Proteomes; UP000244441; 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; 3.40.50.300; 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}; Reference proteome {ECO:0000313|Proteomes:UP000244441}.
FT   BINDING         115..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   364 AA;  39559 MW;  F12AA3AEB9E7BF6B CRC64;
     MDKQSLNMFS KLFRPKKASY ALQTKVEKAL AKYTSNLFPV GLAKVVSNLH IKQQDNGLKL
     SGDMPFPFAS EAEAIVQHLT TKLECAIELN FICQIEPIFQ HEVAGVKNII AVNSGKGGVG
     KSTTTVNLAY ALKALGLKVG VLDADVHGPS MPTMLGLDGQ HPMSPDGKHL LPIEKNGIAV
     MSSGFLADDD GTRIWKGSIS SNAFEQMFKE TIWGDLDVLL IDMPPGTGDI QLTLVQRIPA
     VTSVIVTTPQ DVALLDVQKG LNMFKRLNLP VLGMIENMSY HVCPNCQNQA HIFGDCGGEA
     YAKQVDLPLL GKLPLHIDVR QAADKGQSIQ DSAPDSQLAI AYRQLAEQVC AQQYYQFDSR
     APKS
//
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