SUFC_ECOLI
ID SUFC_ECOLI Reviewed; 248 AA.
AC P77499;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Probable ATP-dependent transporter SufC;
GN Name=sufC; Synonyms=ynhD; OrderedLocusNames=b1682, JW1672;
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, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=12554644; DOI=10.1093/emboj/cdg061;
RA Nachin L., Loiseau L., Expert D., Barras F.;
RT "SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis
RT under oxidative stress.";
RL EMBO J. 22:427-437(2003).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12941942; DOI=10.1074/jbc.m308004200;
RA Outten F.W., Wood M.J., Munoz F.M., Storz G.;
RT "The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase
RT activity as part of a sulfur transfer pathway for Fe-S cluster assembly in
RT Escherichia coli.";
RL J. Biol. Chem. 278:45713-45719(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH SUFA.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=16364320; DOI=10.1016/j.febslet.2005.11.058;
RA Kitaoka S., Wada K., Hasegawa Y., Minami Y., Fukuyama K., Takahashi Y.;
RT "Crystal structure of Escherichia coli SufC, an ABC-type ATPase component
RT of the SUF iron-sulfur cluster assembly machinery.";
RL FEBS Lett. 580:137-143(2006).
CC -!- FUNCTION: Has low ATPase activity. The SufBCD complex acts
CC synergistically with SufE to stimulate the cysteine desulfurase
CC activity of SufS. The SufBCD complex contributes to the assembly or
CC repair of oxygen-labile iron-sulfur clusters under oxidative stress.
CC May facilitate iron uptake from extracellular iron chelators under iron
CC limitation. {ECO:0000269|PubMed:12554644, ECO:0000269|PubMed:12941942,
CC ECO:0000269|PubMed:19810706}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.29 mM for ATP {ECO:0000269|PubMed:12554644};
CC Vmax=4.45 umol/min/mg enzyme {ECO:0000269|PubMed:12554644};
CC -!- SUBUNIT: Part of the SufBCD complex that contains SufB, SufC and SufD.
CC Interacts directly with SufB and SufD. Interacts with SufA
CC (PubMed:19810706). {ECO:0000269|PubMed:12554644,
CC ECO:0000269|PubMed:12941942, ECO:0000269|PubMed:19810706}.
CC -!- INTERACTION:
CC P77499; P77667: sufA; NbExp=5; IntAct=EBI-561601, EBI-1125011;
CC P77499; P77522: sufB; NbExp=15; IntAct=EBI-561601, EBI-562758;
CC P77499; P77689: sufD; NbExp=9; IntAct=EBI-561601, EBI-562751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12554644}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Ycf16 family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74752.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15455.1; -; Genomic_DNA.
DR PIR; B64926; B64926.
DR RefSeq; NP_416197.1; NC_000913.3.
DR RefSeq; WP_000948863.1; NZ_SSZK01000001.1.
DR PDB; 2D3W; X-ray; 2.50 A; A/B/C/D=1-248.
DR PDB; 2ZU0; X-ray; 2.20 A; C/D=1-248.
DR PDB; 5AWF; X-ray; 2.96 A; C/D/G/H=1-248.
DR PDB; 5AWG; X-ray; 4.28 A; C/D/G/H=1-248.
DR PDBsum; 2D3W; -.
DR PDBsum; 2ZU0; -.
DR PDBsum; 5AWF; -.
DR PDBsum; 5AWG; -.
DR AlphaFoldDB; P77499; -.
DR SMR; P77499; -.
DR BioGRID; 4260279; 73.
DR BioGRID; 850488; 2.
DR ComplexPortal; CPX-2123; sufBCD complex.
DR DIP; DIP-10939N; -.
DR IntAct; P77499; 16.
DR MINT; P77499; -.
DR STRING; 511145.b1682; -.
DR jPOST; P77499; -.
DR PaxDb; P77499; -.
DR PRIDE; P77499; -.
DR EnsemblBacteria; AAC74752; AAC74752; b1682.
DR EnsemblBacteria; BAA15455; BAA15455; BAA15455.
DR GeneID; 946128; -.
DR KEGG; ecj:JW1672; -.
DR KEGG; eco:b1682; -.
DR PATRIC; fig|1411691.4.peg.576; -.
DR EchoBASE; EB3722; -.
DR eggNOG; COG0396; Bacteria.
DR HOGENOM; CLU_000604_48_1_6; -.
DR InParanoid; P77499; -.
DR OMA; MAMLEPK; -.
DR PhylomeDB; P77499; -.
DR BioCyc; EcoCyc:G6908-MON; -.
DR EvolutionaryTrace; P77499; -.
DR PRO; PR:P77499; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR CDD; cd03217; ABC_FeS_Assembly; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR010230; FeS-cluster_ATPase_SufC.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43204; PTHR43204; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01978; sufC; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..248
FT /note="Probable ATP-dependent transporter SufC"
FT /id="PRO_0000092980"
FT DOMAIN 2..246
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 14..24
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2D3W"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:2ZU0"
FT TURN 135..139
FT /evidence="ECO:0007829|PDB:2ZU0"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2ZU0"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:2ZU0"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:2ZU0"
SQ SEQUENCE 248 AA; 27582 MW; 78FB1108E1850DF9 CRC64;
MLSIKDLHVS VEDKAILRGL SLDVHPGEVH AIMGPNGSGK STLSATLAGR EDYEVTGGTV
EFKGKDLLAL SPEDRAGEGI FMAFQYPVEI PGVSNQFFLQ TALNAVRSYR GQETLDRFDF
QDLMEEKIAL LKMPEDLLTR SVNVGFSGGE KKRNDILQMA VLEPELCILD ESDSGLDIDA
LKVVADGVNS LRDGKRSFII VTHYQRILDY IKPDYVHVLY QGRIVKSGDF TLVKQLEEQG
YGWLTEQQ
