APBC_SALTY
ID APBC_SALTY Reviewed; 369 AA.
AC Q8ZNN5;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040, ECO:0000305};
GN Name=apbC {ECO:0000303|PubMed:12486045};
GN Synonyms=mrp {ECO:0000312|EMBL:AAL21057.1};
GN OrderedLocusNames=STM2154 {ECO:0000312|EMBL:AAL21057.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION AS AN ATPASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=12486045; DOI=10.1128/jb.185.1.98-106.2003;
RA Skovran E., Downs D.M.;
RT "Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster
RT metabolism in Salmonella enterica serovar Typhimurium.";
RL J. Bacteriol. 185:98-106(2003).
RN [3]
RP FUNCTION, AND SUBUNIT.
RX PubMed=18616280; DOI=10.1021/bi800551y;
RA Boyd J.M., Pierik A.J., Netz D.J., Lill R., Downs D.M.;
RT "Bacterial ApbC can bind and effectively transfer iron-sulfur clusters.";
RL Biochemistry 47:8195-8202(2008).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF LYS-116; LYS-121; SER-122; SER-182; CYS-283
RP AND CYS-286.
RC STRAIN=LT2;
RX PubMed=19001370; DOI=10.1074/jbc.m807003200;
RA Boyd J.M., Sondelski J.L., Downs D.M.;
RT "Bacterial ApbC protein has two biochemical activities that are required
RT for in vivo function.";
RL J. Biol. Chem. 284:110-118(2009).
CC -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC apoproteins (PubMed:18616280, PubMed:19001370). Can hydrolyze ATP
CC (PubMed:12486045, PubMed:19001370). Both activities are required for
CC function in vivo, but the ability to hydrolyze ATP is not necessary for
CC Fe-S cluster transfer (PubMed:19001370). {ECO:0000269|PubMed:12486045,
CC ECO:0000269|PubMed:18616280, ECO:0000269|PubMed:19001370}.
CC -!- SUBUNIT: Homodimer. Holo-ApbC forms a mixture of homodimers and
CC homotetramers. {ECO:0000269|PubMed:18616280}.
CC -!- DISRUPTION PHENOTYPE: Mutants are impaired in Fe-S cluster metabolism.
CC They are conditional thiamine auxotrophs and have lower aconitase and
CC succinate dehydrogenase activities. {ECO:0000269|PubMed:12486045}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC {ECO:0000255|HAMAP-Rule:MF_02040, ECO:0000305}.
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DR EMBL; AE006468; AAL21057.1; -; Genomic_DNA.
DR RefSeq; NP_461098.1; NC_003197.2.
DR RefSeq; WP_001005424.1; NC_003197.2.
DR AlphaFoldDB; Q8ZNN5; -.
DR SMR; Q8ZNN5; -.
DR STRING; 99287.STM2154; -.
DR PaxDb; Q8ZNN5; -.
DR DNASU; 1253675; -.
DR EnsemblBacteria; AAL21057; AAL21057; STM2154.
DR GeneID; 1253675; -.
DR KEGG; stm:STM2154; -.
DR PATRIC; fig|99287.12.peg.2279; -.
DR HOGENOM; CLU_024839_0_0_6; -.
DR OMA; NMAYFTP; -.
DR PhylomeDB; Q8ZNN5; -.
DR BioCyc; SENT99287:STM2154-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
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; PF10609; ParA; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..369
FT /note="Iron-sulfur cluster carrier protein"
FT /id="PRO_0000433952"
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
FT MUTAGEN 116
FT /note="K->A: Hydrolyzes ATP and can bind an Fe-S cluster,
FT but cluster transfer is compromised."
FT /evidence="ECO:0000269|PubMed:19001370"
FT MUTAGEN 121
FT /note="K->A: Hydrolyzes ATP and can bind an Fe-S cluster,
FT but cluster transfer is compromised."
FT /evidence="ECO:0000269|PubMed:19001370"
FT MUTAGEN 122
FT /note="S->A: Can bind and transfer an Fe-S cluster, but has
FT no detectable ATPase activity."
FT /evidence="ECO:0000269|PubMed:19001370"
FT MUTAGEN 182
FT /note="S->A: Can bind and transfer an Fe-S cluster, but has
FT no detectable ATPase activity."
FT /evidence="ECO:0000269|PubMed:19001370"
FT MUTAGEN 283
FT /note="C->A: Can hydrolyze ATP and transfer an Fe-S
FT cluster."
FT /evidence="ECO:0000269|PubMed:19001370"
FT MUTAGEN 286
FT /note="C->A: Can hydrolyze ATP and transfer an Fe-S
FT cluster."
FT /evidence="ECO:0000269|PubMed:19001370"
SQ SEQUENCE 369 AA; 39930 MW; 16AF18AF06B101C6 CRC64;
MNEQSQAKSP DTLRAMVAGT LANFQHPTLK HNLTTLKALH HVAWMDDTLH VELVMPFVWN
SAFEVLKEQC SADLLRITGA KAIDWKLSYN IATLKRVKNQ PGINGVKNII AVSSGKGGVG
KSSTAVNLAL ALAAEGAKVG VLDADIYGPS IPTMLGAEDQ RPTSPDGTHM APIMSHGLAT
NSIGYLVTDD NAMVWRGPMA SKALMQMLQE TLWPDLDYLV LDMPPGTGDI QLTLAQNIPV
TGAVVVTTPQ DIALIDAKKG IVMFEKVEVP VLGIVENMSM HICSNCGHHE PIFGTGGAQK
LAEKYHTQLL GQMPLHISLR EDLDRGTPTV VSRPESEFTA IYRELADRVA AQLYWQGEVI
PGEIAFRAV
