ID A0A256BB27_9CYAN Unreviewed; 369 AA.
AC A0A256BB27;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=B9G53_20630 {ECO:0000313|EMBL:OYQ62724.1};
OS Pseudanabaena sp. SR411.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=1980935 {ECO:0000313|EMBL:OYQ62724.1, ECO:0000313|Proteomes:UP000215660};
RN [1] {ECO:0000313|EMBL:OYQ62724.1, ECO:0000313|Proteomes:UP000215660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR411 {ECO:0000313|EMBL:OYQ62724.1,
RC ECO:0000313|Proteomes:UP000215660};
RA Stowe E.L., Hundermark E.L., Stowe W.;
RT "Novel uncharacterized cyanobacterium from Susquehanna River.";
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYQ62724.1}.
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DR EMBL; NDHW01000193; OYQ62724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256BB27; -.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000215660; 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}; Reference proteome {ECO:0000313|Proteomes:UP000215660}.
FT DOMAIN 29..96
FT /note="MIP18 family-like"
FT /evidence="ECO:0000259|Pfam:PF01883"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 369 AA; 39758 MW; B7F522236EC98140 CRC64;
MPSHTSPFQR AEHPVPPPTD PQVEVKELAV KSLLKTVIEP ILNMDIVSLG MVRNLRIVDD
YVYLRLYVGK HQFALKAQIM ELLSSSLDWC KKSYVEVCTI AGVRTTIAVS SGKGGVGKST
TAVNLAAALR SQGNKVGLLD ADVYGPNVPQ MLGLAQEDVK VIDTPTGQRF IPLEAHGIKV
MSVGLLAAPD HPLAWRGPVL HKIITQFIQE VEWGDLDYLL IDLPPGTGDA QITIVQESPI
CGVILVTTPQ QVAVADVRRS IHMFRRVGIP VLGIIENMSY LLCGHCGTPN PIFGSGGGQQ
LADELQAPLL GQVPIDAKIC TGGDIGTPLT LSEPHSAVAE VFTKIAIALD NSFAEHNTNS
REFDNTFVN
//
