SUFT_STAA3
ID SUFT_STAA3 Reviewed; 88 AA.
AC A0A0H2XI17;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Fe-S protein maturation auxiliary factor SufT {ECO:0000303|PubMed:27517714};
DE AltName: Full=Fe-S protein maturation accessory factor SufT {ECO:0000303|PubMed:27517714};
DE AltName: Full=Iron-sulfur cluster assembly factor SufT {ECO:0000303|PubMed:27671355};
GN Name=sufT {ECO:0000303|PubMed:27517714, ECO:0000303|PubMed:27671355};
GN OrderedLocusNames=SAUSA300_0875 {ECO:0000312|EMBL:ABD22304.1};
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=USA300;
RX PubMed=27671355; DOI=10.1111/mmi.13539;
RA Mashruwala A.A., Roberts C.A., Bhatt S., May K.L., Carroll R.K., Shaw L.N.,
RA Boyd J.M.;
RT "Staphylococcus aureus SufT: an essential iron-sulphur cluster assembly
RT factor in cells experiencing a high-demand for lipoic acid.";
RL Mol. Microbiol. 102:1099-1119(2016).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=USA300;
RX PubMed=27517714; DOI=10.1371/journal.pgen.1006233;
RA Mashruwala A.A., Bhatt S., Poudel S., Boyd E.S., Boyd J.M.;
RT "The DUF59 containing protein SufT is involved in the maturation of iron-
RT sulfur (FeS) proteins during conditions of high FeS cofactor demand in
RT Staphylococcus aureus.";
RL PLoS Genet. 12:E1006233-E1006233(2016).
CC -!- FUNCTION: Involved in the maturation of iron-sulfur (Fe-S) proteins
CC (PubMed:27671355, PubMed:27517714). May function as a Fe-S cluster
CC carrier (PubMed:27671355). Is required for S.aureus growth under
CC conditions that impose a high demand for lipoic acid, likely via a role
CC in the maturation of the lipoate synthase LipA (PubMed:27671355). Is
CC non-essential for growth in conditions that impose a low demand for
CC lipoic acid or Fe-S clusters, such as fermentative growth
CC (PubMed:27671355, PubMed:27517714). Seems also to be involved in the
CC maturation of AcnA, LeuCD and IlvD proteins, that utilize Fe-S cluster
CC cofactors, and its role increases under conditions of high-demand for
CC Fe-S clusters (respiratory growth) (PubMed:27517714). Is not involved
CC in the repair of Fe-S clusters damaged by reactive oxygen species or in
CC the physical protection of Fe-S clusters from oxidants
CC (PubMed:27517714). Displays synergy with the Fe-S cluster carrier Nfu
CC (PubMed:27517714). {ECO:0000269|PubMed:27517714,
CC ECO:0000269|PubMed:27671355}.
CC -!- INDUCTION: Transcription of sufT decreases when aerobically cultured
CC cells are shifted to an anaerobic (fermentative) environment, and
CC increases upon reaeration (PubMed:27517714). Up-regulated upon culture
CC in serine dropout medium relative to liquid 20 AA medium
CC (PubMed:27671355). {ECO:0000269|PubMed:27517714,
CC ECO:0000269|PubMed:27671355}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have decreased activities
CC of the Fe-S cluster-dependent enzymes AcnA, LeuCD and IlvD, meaning a
CC defect in the assembly of Fe-S proteins (PubMed:27517714). They are
CC capable of growth in liquid chemically defined medium containing the 20
CC canonical amino acids (AA) and glucose as a carbon source, but display
CC growth defects in defined medium lacking leucine and isoleucine
CC (PubMed:27517714). In contrast, the deletion mutant strain is unable to
CC grow upon the same 20 AA medium in solid form; supplementation of the
CC solid 20 AA medium with lipoic acid fully corrects the growth of the
CC mutant strain, and returning the sufT gene in trans also corrects
CC growth in the absence of lipoic acid (PubMed:27671355). Further
CC experimentation found that S.aureus growth upon solid chemically
CC defined media was highly reliant upon the lipoamide-requiring enzymes
CC pyruvate dehydrogenase (Pdh) and branched chain keto-acid dehydrogenase
CC (Bck); the reliance upon Pdh and Bck for growth was decreased upon
CC culture in liquid defined media (PubMed:27671355). A strain lacking
CC SufT displays phenotypes consistent with decreased activities of
CC multiple lipoamide-dependent enzymes (LipA, Pdh, Bck and Gcv)
CC (PubMed:27671355). {ECO:0000269|PubMed:27517714,
CC ECO:0000269|PubMed:27671355}.
CC -!- SIMILARITY: Belongs to the MIP18 family. {ECO:0000305}.
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DR EMBL; CP000255; ABD22304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H2XI17; -.
DR SMR; A0A0H2XI17; -.
DR EnsemblBacteria; ABD22304; ABD22304; SAUSA300_0875.
DR KEGG; saa:SAUSA300_0875; -.
DR HOGENOM; CLU_091588_2_2_9; -.
DR Proteomes; UP000001939; Chromosome.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR002744; MIP18-like.
DR Pfam; PF01883; FeS_assembly_P; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 2: Evidence at transcript level;
FT CHAIN 1..88
FT /note="Fe-S protein maturation auxiliary factor SufT"
FT /id="PRO_0000439588"
SQ SEQUENCE 88 AA; 9652 MW; 7CD0420BEE8E70F4 CRC64;
MVIDPELGID IVNLGLVYKV NVDDEGVCTV DMTLTSMGCP MGPQIIDQVK TVLAEIPEIQ
DTEVNIVWSP PWTKDMMSRY AKIALGVS
