APBC_MYCBO
ID APBC_MYCBO Reviewed; 381 AA.
AC P65442; A0A1R3XZW0; O33225; X2BHF8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN Name=mrp; OrderedLocusNames=BQ2027_MB1261C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MIP18 family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the Mrp/NBP35 ATP-
CC binding proteins family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SIT99862.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; LT708304; SIT99862.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_854915.1; NC_002945.3.
DR AlphaFoldDB; P65442; -.
DR SMR; P65442; -.
DR EnsemblBacteria; SIT99862; SIT99862; BQ2027_MB1261C.
DR PATRIC; fig|233413.5.peg.1384; -.
DR Proteomes; UP000001419; 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 Gene3D; 3.30.300.130; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR002744; MIP18-like.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR044304; NUBPL-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR42961; PTHR42961; 1.
DR Pfam; PF01883; FeS_assembly_P; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..381
FT /note="Iron-sulfur cluster carrier protein"
FT /id="PRO_0000184939"
FT BINDING 125..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ SEQUENCE 381 AA; 40084 MW; 4EEB863B79D6B91A CRC64;
MSGTRDGDLN AAIRTALGKV IDPELRRPIT ELGMVKSIDT GPDGSVHVEI YLTIAGCPKK
SEITERVTRA VADVPGTSAV RVSLDVMSDE QRTELRKQLR GDTREPVIPF AQPDSLTRVY
AVASGKGGVG KSTVTVNLAA AMAVRGLSIG VLDADIHGHS IPRMMGTTDR PTQVESMILP
PIAHQVKVIS IAQFTQGNTP VVWRGPMLHR ALQQFLADVY WGDLDVLLLD LPPGTGDVAI
SVAQLIPNAE LLVVTTPQLA AAEVAERAGS IALQTRQRIV GVVENMSGLT LPDGTTMQVF
GEGGGRLVAE RLSRAVGADV PLLGQIPLDP ALVAAGDSGV PLVLSSPDSA IGKELHSIAD
GLSTRRRGLA GMSLGLDPTR R