SUFA_ECOLI
ID SUFA_ECOLI Reviewed; 122 AA.
AC P77667;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein SufA;
GN Name=sufA; Synonyms=ydiC; OrderedLocusNames=b1684, JW1674;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP GENE NAME.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10322040; DOI=10.1128/jb.181.10.3307-3309.1999;
RA Patzer S.I., Hantke K.;
RT "SufS is a NifS-like protein, and SufD is necessary for stability of the
RT 2Fe-2S FhuF protein in Escherichia coli.";
RL J. Bacteriol. 181:3307-3309(1999).
RN [5]
RP FUNCTION, MUTAGENESIS OF CYS-50; CYS-114 AND CYS-116, AND SULFUR-BINDING.
RX PubMed=17350000; DOI=10.1016/j.febslet.2007.02.058;
RA Sendra M., Ollagnier de Choudens S., Lascoux D., Sanakis Y., Fontecave M.;
RT "The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from
RT the SUFS-SUFE complex to SUFA.";
RL FEBS Lett. 581:1362-1368(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17941825; DOI=10.1042/bj20071166;
RA Lu J., Yang J., Tan G., Ding H.;
RT "Complementary roles of SufA and IscA in the biogenesis of iron-sulfur
RT clusters in Escherichia coli.";
RL Biochem. J. 409:535-543(2008).
RN [7]
RP FUNCTION.
RX PubMed=19366265; DOI=10.1021/ja807551e;
RA Gupta V., Sendra M., Naik S.G., Chahal H.K., Huynh B.H., Outten F.W.,
RA Fontecave M., Ollagnier de Choudens S.;
RT "Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a
RT [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes.";
RL J. Am. Chem. Soc. 131:6149-6153(2009).
RN [8]
RP FUNCTION, AND INTERACTION WITH SUFB AND SUFC.
RX PubMed=19810706; DOI=10.1021/bi901518y;
RA Chahal H.K., Dai Y., Saini A., Ayala-Castro C., Outten F.W.;
RT "The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster
RT transfer.";
RL Biochemistry 48:10644-10653(2009).
RN [9]
RP FUNCTION.
RX PubMed=23018275; DOI=10.1016/j.jinorgbio.2012.06.008;
RA Chahal H.K., Outten F.W.;
RT "Separate FeS scaffold and carrier functions for SufB(2)C(2) and SufA
RT during in vitro maturation of [2Fe2S] Fdx.";
RL J. Inorg. Biochem. 116:126-134(2012).
RN [10] {ECO:0007744|PDB:2D2A}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16298366; DOI=10.1016/j.febslet.2005.10.046;
RA Wada K., Hasegawa Y., Gong Z., Minami Y., Fukuyama K., Takahashi Y.;
RT "Crystal structure of Escherichia coli SufA involved in biosynthesis of
RT iron-sulfur clusters: implications for a functional dimer.";
RL FEBS Lett. 579:6543-6548(2005).
CC -!- FUNCTION: Member of gene cluster sufABCDSE that mediates iron-sulfur
CC cluster assembly under oxidative stress and iron limitation conditions
CC (PubMed:17941825). Binds [2Fe2S] cluster by mobilizing sulfur atoms
CC provided by the SufS-SufE cysteine desulfurase system and then
CC transfers the assembled Fe-S cluster to target proteins including
CC ferredoxin and aconitase (PubMed:17350000, PubMed:19366265). Seems to
CC act as a Fe-S cluster carrier rather than a scaffold, this role being
CC performed by SufB and SufC (PubMed:19810706, PubMed:23018275).
CC {ECO:0000269|PubMed:17350000, ECO:0000269|PubMed:17941825,
CC ECO:0000269|PubMed:19366265, ECO:0000269|PubMed:19810706,
CC ECO:0000269|PubMed:23018275}.
CC -!- SUBUNIT: Homodimer (PubMed:16298366). Interacts with SufB and SufC
CC (PubMed:19810706). {ECO:0000269|PubMed:16298366,
CC ECO:0000269|PubMed:19810706}.
CC -!- INTERACTION:
CC P77667; P77522: sufB; NbExp=5; IntAct=EBI-1125011, EBI-562758;
CC P77667; P77499: sufC; NbExp=5; IntAct=EBI-1125011, EBI-561601;
CC -!- DISRUPTION PHENOTYPE: Deletion has only a mild effect on cell growth
CC (PubMed:17941825). However, deletion of both IscA and SufA results in a
CC severe growth phenotype in minimal medium under aerobic growth
CC conditions (PubMed:17941825). {ECO:0000269|PubMed:17941825}.
CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
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DR EMBL; U00096; AAC74754.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15453.1; -; Genomic_DNA.
DR PIR; D64926; D64926.
DR RefSeq; NP_416199.1; NC_000913.3.
DR RefSeq; WP_000367160.1; NZ_STEB01000003.1.
DR PDB; 2D2A; X-ray; 2.70 A; A/B=1-122.
DR PDBsum; 2D2A; -.
DR AlphaFoldDB; P77667; -.
DR BMRB; P77667; -.
DR SMR; P77667; -.
DR BioGRID; 4260283; 48.
DR ComplexPortal; CPX-2142; sufA complex.
DR IntAct; P77667; 8.
DR STRING; 511145.b1684; -.
DR jPOST; P77667; -.
DR PaxDb; P77667; -.
DR PRIDE; P77667; -.
DR EnsemblBacteria; AAC74754; AAC74754; b1684.
DR EnsemblBacteria; BAA15453; BAA15453; BAA15453.
DR GeneID; 66674423; -.
DR GeneID; 949014; -.
DR KEGG; ecj:JW1674; -.
DR KEGG; eco:b1684; -.
DR PATRIC; fig|1411691.4.peg.574; -.
DR EchoBASE; EB1352; -.
DR eggNOG; COG0316; Bacteria.
DR HOGENOM; CLU_069054_4_2_6; -.
DR InParanoid; P77667; -.
DR OMA; DFAWRGL; -.
DR PhylomeDB; P77667; -.
DR BioCyc; EcoCyc:EG11378-MON; -.
DR EvolutionaryTrace; P77667; -.
DR PRO; PR:P77667; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990230; C:iron-sulfur cluster transfer complex; IPI:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:EcoCyc.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:ComplexPortal.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR Gene3D; 2.60.300.12; -; 1.
DR InterPro; IPR000361; FeS_biogenesis.
DR InterPro; IPR016092; FeS_cluster_insertion.
DR InterPro; IPR017870; FeS_cluster_insertion_CS.
DR InterPro; IPR035903; HesB-like_dom_sf.
DR InterPro; IPR011298; SufA_proteobacteria.
DR Pfam; PF01521; Fe-S_biosyn; 1.
DR SUPFAM; SSF89360; SSF89360; 1.
DR TIGRFAMs; TIGR01997; sufA_proteo; 1.
DR TIGRFAMs; TIGR00049; TIGR00049; 1.
DR PROSITE; PS01152; HESB; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..122
FT /note="Protein SufA"
FT /id="PRO_0000076987"
FT BINDING 114
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:16298366,
FT ECO:0000305|PubMed:17350000"
FT BINDING 116
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:16298366,
FT ECO:0000305|PubMed:17350000"
FT MUTAGEN 50
FT /note="C->S: Decrease of sulfur binding activity."
FT /evidence="ECO:0000269|PubMed:17350000"
FT MUTAGEN 114
FT /note="C->S: Strong decrease of sulfur binding activity."
FT /evidence="ECO:0000269|PubMed:17350000"
FT MUTAGEN 116
FT /note="C->S: Strong decrease of sulfur binding activity."
FT /evidence="ECO:0000269|PubMed:17350000"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:2D2A"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:2D2A"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2D2A"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:2D2A"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2D2A"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2D2A"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2D2A"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:2D2A"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:2D2A"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2D2A"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2D2A"
SQ SEQUENCE 122 AA; 13300 MW; D26817F42E4B740B CRC64;
MDMHSGTFNP QDFAWQGLTL TPAAAIHIRE LVAKQPGMVG VRLGVKQTGC AGFGYVLDSV
SEPDKDDLLF EHDGAKLFVP LQAMPFIDGT EVDFVREGLN QIFKFHNPKA QNECGCGESF
GV
