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Database: UniProt
Entry: A0A1Y0KPJ6_9PSED
LinkDB: A0A1Y0KPJ6_9PSED
Original site: A0A1Y0KPJ6_9PSED 
ID   A0A1Y0KPJ6_9PSED        Unreviewed;       363 AA.
AC   A0A1Y0KPJ6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, 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=B9K09_06225 {ECO:0000313|EMBL:ARU87586.1};
OS   Pseudomonas sp. M30-35.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1981174 {ECO:0000313|EMBL:ARU87586.1, ECO:0000313|Proteomes:UP000196445};
RN   [1] {ECO:0000313|EMBL:ARU87586.1, ECO:0000313|Proteomes:UP000196445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M30-35 {ECO:0000313|EMBL:ARU87586.1,
RC   ECO:0000313|Proteomes:UP000196445};
RA   He A., Zhao Q., Li H., Zhang J.;
RT   "Complete genome sequence of the plant growth-promoting rhizobacterium
RT   Pseudomonas rhizovicinus strain M30-35.";
RL   Submitted (APR-2017) 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; CP020892; ARU87586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0KPJ6; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000196445; 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:UP000196445}.
FT   DOMAIN          6..77
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   BINDING         106..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   363 AA;  38432 MW;  2302208AD427CB17 CRC64;
     MSVTREVVEA TLRQYTDPHL NQDPVSAGCL REIDIQGRQV NVRLELGYAA GLFKSGWAQV
     LEMALTNLEG IDAAKVQIDC VIAAHKAQEQ VPALANVKNI IAVASGKGGV GKSTTAANLA
     LALAREGAKV GILDADIYGP SQGIMFGIAE GTRPLVKDQK WFVPLEAHGV EVMSMAFLTD
     ENTPVVWRGP MVSGALIQLI TQTAWTDLDY LVVDMPPGTG DIQLTLAQKV PVAGAVIVTT
     PQDLALLDAK KGVEMFRKVN IPVLGVVENM AVHICSNCGH AEHLFGEGGG EKLAKQFDVD
     LLASLPLSMA IRMQSDGGKP TTIADPESQI AMIYQETART VGARIAQSGA TAQAMPTISV
     SDD
//
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