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Database: UniProt
Entry: A0A1H2VGT6_9FLAO
LinkDB: A0A1H2VGT6_9FLAO
Original site: A0A1H2VGT6_9FLAO 
ID   A0A1H2VGT6_9FLAO        Unreviewed;       379 AA.
AC   A0A1H2VGT6;
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=SAMN04487892_2078 {ECO:0000313|EMBL:SDW67595.1};
OS   Allomuricauda zhangzhouensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=1073328 {ECO:0000313|EMBL:SDW67595.1, ECO:0000313|Proteomes:UP000199592};
RN   [1] {ECO:0000313|Proteomes:UP000199592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25030 {ECO:0000313|Proteomes:UP000199592};
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; FNMY01000002; SDW67595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2VGT6; -.
DR   STRING; 1073328.SAMN05216294_0215; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000199592; 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          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;  40891 MW;  5C723A6400C789C4 CRC64;
     MKLKKADILK ALEKISAPGE GQNLVESGAV TNIQVFGDEV EVDVTIKNPS LQAKKKTEVE
     ILKCIHREVY EKAKIKVNLK VDAPATPKVN QIKGNPIPGI QNIVAVASGK GGVGKSTITA
     NLAVTLAKMG FKVGLLDTDI YGPSMPIMFD VANEKPLSVN VDGKAKMKPI ENYGVKLLSI
     GFFTQPNQAV IWRGPMAAKA LNQMIFDAHW GELDFLLLDL PPGTGDIHLS IMQSMPVTGA
     VVVSTPQEIA LADARKGVAM FQQEAINVPV LGIVENMAYF TPEELPENKY YIFGQHGAKN
     LAEDLDVPFL GEVPLVQSIR EAGDVGRPAA MQTATPIEEA FEEITKQVVQ EVVKRNTDLP
     PTEAIKITTM AGCSAVKKK
//
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