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   18-SEP-2019, entry version 153.
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.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   GENE NAME.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=10322040;
RA   Patzer S.I., Hantke K.;
RT   "SufS is a NifS-like protein, and SufD is necessary for stability of
RT   the 2Fe-2S FhuF protein in Escherichia coli.";
RL   J. Bacteriol. 181:3307-3309(1999).
RN   [5]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT,
RP   BIOPHYSICOCHEMICAL 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]
RT   biogenesis 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
RT   desulfurase activity as part of a sulfur transfer pathway for Fe-S
RT   cluster assembly in Escherichia coli.";
RL   J. Biol. Chem. 278:45713-45719(2003).
RN   [7]
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.,
RA   Takahashi Y.;
RT   "Crystal structure of Escherichia coli SufC, an ABC-type ATPase
RT   component 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
CC       or repair of oxygen-labile iron-sulfur clusters under oxidative
CC       stress. May facilitate iron uptake from extracellular iron
CC       chelators under iron limitation. {ECO:0000269|PubMed:12554644,
CC       ECO:0000269|PubMed:12941942}.
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
CC       SufD. Interacts directly with SufB and SufD.
CC       {ECO:0000269|PubMed:12554644, ECO:0000269|PubMed:12941942}.
CC   -!- INTERACTION:
CC       P77667:sufA; NbExp=5; IntAct=EBI-561601, EBI-1125011;
CC       P77522:sufB; NbExp=15; IntAct=EBI-561601, EBI-562758;
CC       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
CC       family. {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   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   EPD; P77499; -.
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   EcoGene; EG13964; sufC.
DR   eggNOG; ENOG4105C3K; Bacteria.
DR   eggNOG; COG0396; LUCA.
DR   InParanoid; P77499; -.
DR   KO; K09013; -.
DR   PhylomeDB; P77499; -.
DR   BioCyc; EcoCyc:G6908-MONOMER; -.
DR   BioCyc; ECOL316407:JW1672-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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase 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   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR010230; FeS-cluster_ATPase_SufC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43204:SF1; PTHR43204:SF1; 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; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN         1    248       Probable ATP-dependent transporter SufC.
FT                                /FTId=PRO_0000092980.
FT   DOMAIN        2    246       ABC transporter. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   NP_BIND      34     41       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   STRAND        2     11       {ECO:0000244|PDB:2ZU0}.
FT   STRAND       14     24       {ECO:0000244|PDB:2ZU0}.
FT   STRAND       29     33       {ECO:0000244|PDB:2ZU0}.
FT   HELIX        40     48       {ECO:0000244|PDB:2ZU0}.
FT   STRAND       54     62       {ECO:0000244|PDB:2ZU0}.
FT   HELIX        67     69       {ECO:0000244|PDB:2ZU0}.
FT   HELIX        72     78       {ECO:0000244|PDB:2ZU0}.
FT   STRAND       80     83       {ECO:0000244|PDB:2ZU0}.
FT   STRAND       88     90       {ECO:0000244|PDB:2D3W}.
FT   HELIX        95    108       {ECO:0000244|PDB:2ZU0}.
FT   HELIX       109    111       {ECO:0000244|PDB:2ZU0}.
FT   HELIX       117    130       {ECO:0000244|PDB:2ZU0}.
FT   TURN        135    139       {ECO:0000244|PDB:2ZU0}.
FT   TURN        142    145       {ECO:0000244|PDB:2ZU0}.
FT   HELIX       148    162       {ECO:0000244|PDB:2ZU0}.
FT   STRAND      165    171       {ECO:0000244|PDB:2ZU0}.
FT   TURN        172    175       {ECO:0000244|PDB:2ZU0}.
FT   HELIX       178    189       {ECO:0000244|PDB:2ZU0}.
FT   STRAND      197    201       {ECO:0000244|PDB:2ZU0}.
FT   HELIX       205    209       {ECO:0000244|PDB:2ZU0}.
FT   STRAND      214    220       {ECO:0000244|PDB:2ZU0}.
FT   STRAND      223    228       {ECO:0000244|PDB:2ZU0}.
FT   HELIX       232    237       {ECO:0000244|PDB:2ZU0}.
FT   TURN        238    240       {ECO:0000244|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
//