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Database: UniProt
Entry: A0A1Y3CGV0_9GAMM
LinkDB: A0A1Y3CGV0_9GAMM
Original site: A0A1Y3CGV0_9GAMM 
ID   A0A1Y3CGV0_9GAMM        Unreviewed;       424 AA.
AC   A0A1Y3CGV0;
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=B9T28_09110 {ECO:0000313|EMBL:OTG65596.1};
OS   Acinetobacter silvestris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1977882 {ECO:0000313|EMBL:OTG65596.1, ECO:0000313|Proteomes:UP000242765};
RN   [1] {ECO:0000313|EMBL:OTG65596.1, ECO:0000313|Proteomes:UP000242765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 4999 {ECO:0000313|EMBL:OTG65596.1,
RC   ECO:0000313|Proteomes:UP000242765};
RA   Nemec A., Radolfova-Krizova L.;
RT   "High diversity of culturable Acinetobacter species in natural soil and
RT   water ecosystems.";
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   -!- 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:OTG65596.1}.
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DR   EMBL; NEGB01000004; OTG65596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3CGV0; -.
DR   STRING; 1977882.B9T28_09110; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000242765; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
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; PF10609; ParA; 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   REGION          96..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         177..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   424 AA;  45737 MW;  9F839F34C16FE2F5 CRC64;
     MSWLSSLKSV FSPAQEVKEE EIQNVLQSYI LPNSKNALQD RISQINVEGR TLQITINTLP
     AEADQLQQIH DDLADALEKC GIQELNMHVI QQKHNQGDAC SSHDHAKEGH SCSTQPKAET
     KQQANLPPVI DASGASKPEE SQAEIDPNNP PIQKATPQQR DVPKHPRIQN VILVSSGKGG
     VGKSTTTVNL ALALQQLGLK VGVLDADIYG PSIPTMLGNQ GRTPMIEAEN FVPIDAYGLA
     VLSIGHLTGD HNTPVAWRGP KATGALMQLF NQTLWPELDV LVIDMPPGTG DIQLTLAQRI
     PVTAAIIVTT PQNVALMDAT KGIELFNRVH IPVMGVIENM STHICSNCGH EEQIFGTGGG
     DKLAEQYDIP LLGRLPLNVR IRENADAGKP SVIAGDDAAE SYLAIAKKVI DALPKAEKDQ
     SRIF
//
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