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   24-JAN-2024, entry version 174.
DE   RecName: Full=Probable ATP-dependent transporter SufC;
GN   Name=sufC; Synonyms=ynhD; OrderedLocusNames=b1682, JW1672;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; 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; 511145-b1682; -.
DR   EnsemblBacteria; AAC74752; AAC74752; b1682.
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   OrthoDB; 9806149at2; -.
DR   PhylomeDB; P77499; -.
DR   BioCyc; EcoCyc:G6908-MONOMER; -.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR01978; sufC; 1.
DR   PANTHER; PTHR43204; ABC TRANSPORTER I FAMILY MEMBER 6, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43204:SF1; ABC TRANSPORTER I FAMILY MEMBER 6, CHLOROPLASTIC; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//