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Database: UniProt
Entry: A0A1H1QSD5_9FLAO
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Original site: A0A1H1QSD5_9FLAO 
ID   A0A1H1QSD5_9FLAO        Unreviewed;       379 AA.
AC   A0A1H1QSD5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=SAMN04489797_1219 {ECO:0000313|EMBL:SDS26325.1};
OS   Winogradskyella sediminis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1382466 {ECO:0000313|EMBL:SDS26325.1, ECO:0000313|Proteomes:UP000198963};
RN   [1] {ECO:0000313|EMBL:SDS26325.1, ECO:0000313|Proteomes:UP000198963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA_55 {ECO:0000313|EMBL:SDS26325.1,
RC   ECO:0000313|Proteomes:UP000198963};
RA   Varghese N., Submissions S.;
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; LT629774; SDS26325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1QSD5; -.
DR   STRING; 1249933.SAMN04489797_1219; -.
DR   Proteomes; UP000198963; Chromosome I.
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          5..54
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;  40516 MW;  1AECDF25AD7CC721 CRC64;
     MKLNKQDILN ALKTITAPGE GENMVDSGAV TNVVTFADEV IVDITIKNPS LQARKKTEVE
     ILQTIHKEVY EKAKIKVNVK VDAKAAQPKN EIKGKAIPGI QNIVAVASGK GGVGKSTVTA
     NLAVTLAKMG FKVGVLDADI YGPSIPIMFD VANERPLSVN VDGKSKMKPV ENYGVKVLSI
     GFFTKPDQAV IWRGPMASKA LNQMIFDAAW GELDFLLLDL PPGTGDIHLS IMQALPITGS
     VVVSTPQNVA LADAKKGVAM FQQDSINVPV LGIIENMAYF TPAELPENKY YIFGKEGAKH
     LAEDLKVPFL GEVPLVQSIR EAGDLGRPAA MQTATPTEAA FEAITREVVQ QVVNRNEALP
     ATEAIKITTM AGCSAANKK
//
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