ID J1FHL3_9BACT Unreviewed; 367 AA.
AC J1FHL3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=O71_13139 {ECO:0000313|EMBL:EJF09779.1};
OS Pontibacter sp. BAB1700.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1144253 {ECO:0000313|EMBL:EJF09779.1, ECO:0000313|Proteomes:UP000003746};
RN [1] {ECO:0000313|EMBL:EJF09779.1, ECO:0000313|Proteomes:UP000003746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB1700 {ECO:0000313|EMBL:EJF09779.1,
RC ECO:0000313|Proteomes:UP000003746};
RX PubMed=23105068; DOI=10.1128/JB.01550-12;
RA Joshi M.N., Sharma A.C., Pandya R.V., Patel R.P., Saiyed Z.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Pontibacter sp. nov. BAB1700, a Halotolerant,
RT Industrially Important Bacterium.";
RL J. Bacteriol. 194:6329-6330(2012).
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:EJF09779.1}.
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DR EMBL; AKIS01000089; EJF09779.1; -; Genomic_DNA.
DR RefSeq; WP_007656776.1; NZ_AKIS01000089.1.
DR AlphaFoldDB; J1FHL3; -.
DR PATRIC; fig|1144253.3.peg.2593; -.
DR Proteomes; UP000003746; 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..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 367 AA; 39234 MW; E27E6B95DDDCE1F7 CRC64;
MAITKEDILK ALSYVEEPDL GKDLVTLNMI EDVQVDGKNV SFTVILTTPA CPLKDLIRNA
CIRAIHTMVD KEAEVTVNMT SRVTSGRAGS SEVLTGVKNI IAIASGKGGV GKSTVTSNLA
IALAQSGAKV GLIDADIFGP SIPTMFGVED QRPSMVQGDH GKNYIIPVEK YGVKLMSIGF
LTPPDHAVIW RGPMASSALK QFISDVEWGE LDYLLLDLPP GTSDIHLTMV QVLPVTGAVI
VTTPQKVAIA DAQKGLQMFR QPQINVPVLG VVENMAYFTP AELPENKYYI FGQEGGQNLA
KKFDVPVLGQ VPLVQGIREC GDEGTPVALQ NDSPASGVFR ELAQAVAQQV SVRNATLAKT
QPVEIKS
//
