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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//