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Database: UniProt
Entry: A0A3G2LB06_9FLAO
LinkDB: A0A3G2LB06_9FLAO
Original site: A0A3G2LB06_9FLAO 
ID   A0A3G2LB06_9FLAO        Unreviewed;       379 AA.
AC   A0A3G2LB06;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=D1013_19315 {ECO:0000313|EMBL:AYN69381.1};
OS   Euzebyella marina.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Euzebyella.
OX   NCBI_TaxID=1761453 {ECO:0000313|EMBL:AYN69381.1, ECO:0000313|Proteomes:UP000276309};
RN   [1] {ECO:0000313|EMBL:AYN69381.1, ECO:0000313|Proteomes:UP000276309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN62 {ECO:0000313|EMBL:AYN69381.1,
RC   ECO:0000313|Proteomes:UP000276309};
RA   Xue C.;
RT   "The reduced genetic potential of extracellular carbohydrate catabolism in
RT   Euzebyella marina RN62, a Flavobacteriia bacterium isolated from the hadal
RT   water.";
RL   Submitted (AUG-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   -!- 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; CP032050; AYN69381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G2LB06; -.
DR   KEGG; emar:D1013_19315; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000276309; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000276309}.
FT   DOMAIN          5..53
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   BINDING         109..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   379 AA;  40700 MW;  97E95B0082AA0B32 CRC64;
     MKIDKKEVLK ALEHITVPGE GQNMVESGAV KNVQIFGDEV EIDITIGNPS LQARKKTEVE
     ILQVIHREVY EKAKIKVNIK VDAPAKPKVN EIKGKPIPGI QNIVAVASGK GGVGKSTVTA
     NLAVTLAKMG FKVGLLDADI YGPSMPIMFD VANEKPLAVN VAGKSKMKPV ENYGVKLLSI
     GFFTQPNQAV IWRGPMASKA LNQMIFDAAW GELDFLLVDL PPGTGDIHLS IMQAMPITGA
     VVVSTPQEVA LADAKKGVAM FQQESINVPV LGIVENMAYF TPEELPDNKY YIFGKEGAKH
     LSEDLGVPFL GEVPIVQSIR EAGDVGRPAA LQTATPVEEA FEELTKNVVQ EVVGRNKSLP
     PTEAIKITTM AGCSAVKKK
//
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