ID A0A1V3MXC5_9SPHI Unreviewed; 353 AA.
AC A0A1V3MXC5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=BWD42_14670 {ECO:0000313|EMBL:OOG17444.1};
OS Sphingobacterium sp. CZ-UAM.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1933868 {ECO:0000313|EMBL:OOG17444.1, ECO:0000313|Proteomes:UP000188865};
RN [1] {ECO:0000313|EMBL:OOG17444.1, ECO:0000313|Proteomes:UP000188865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CZ-UAM {ECO:0000313|EMBL:OOG17444.1,
RC ECO:0000313|Proteomes:UP000188865};
RA Steffani-Vallejo J.L., Licona-Cassani C., Cruz-Morales P., Lozano L.,
RA Zuniga C., Morales M., Revah S., Utrilla J.;
RT "Genome sequence of Sphingobacterium sp. CZ-UAM, isolated from a
RT methanotrophic consortium.";
RL Submitted (JAN-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:OOG17444.1}.
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DR EMBL; MTCM01000003; OOG17444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3MXC5; -.
DR STRING; 1933868.BWD42_14670; -.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000188865; 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 4..65
FT /note="MIP18 family-like"
FT /evidence="ECO:0000259|Pfam:PF01883"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 353 AA; 37967 MW; BE3645F0F05BB652 CRC64;
MVTKEQILNA LSYVEEPDLK KDLVTLNMIQ NIQIEDQKIA FDVILTTPAC PLKDHIEHAC
RNAIAHFIDK NLEVQINMTS NVVGKQGAQV SGIKNIILVS SGKGGVGKST VAANLALALH
AKGAKTGLLD ADIYGPSLPM MFGLEGAKPG SVEMPDGQVK IEPLEKFGLK LLSIGFFTDP
NQPIPWRGPM TTSAIKQLFN DANWGELDYL VVDMPPGTGD IHITVSQTFP IAGAVIVTTP
QQVALADAVK GIGMFLMDSI NIPLLGVVEN MAYFTPAELP DNKYYIFGKG GGKRLAEEYK
IPFLGEIPLL KGISDAGDNG FPVAIDQEDP VTKSFLTIAE KVAQQLSIIQ SQV
//
