SUFD_ECOLI
ID SUFD_ECOLI Reviewed; 423 AA.
AC P77689;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=FeS cluster assembly protein SufD;
GN Name=sufD; Synonyms=ynhC; OrderedLocusNames=b1681, JW1671;
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 FUNCTION.
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, 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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND SUBUNIT.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: The SufBCD complex acts synergistically with SufE to
CC stimulate the cysteine desulfurase activity of SufS. The SufBCD complex
CC contributes to the assembly or repair of oxygen-labile iron-sulfur
CC clusters under oxidative stress. May facilitate iron uptake from
CC extracellular iron chelators under iron limitation. Required for the
CC stability of the FhuF protein. {ECO:0000269|PubMed:10322040,
CC ECO:0000269|PubMed:12941942}.
CC -!- SUBUNIT: Part of the SufBCD complex that contains SufB, SufC and SufD.
CC Can form homodimers. {ECO:0000269|PubMed:12941942,
CC ECO:0000269|PubMed:16021622}.
CC -!- INTERACTION:
CC P77689; P77522: sufB; NbExp=15; IntAct=EBI-562751, EBI-562758;
CC P77689; P77499: sufC; NbExp=9; IntAct=EBI-562751, EBI-561601;
CC -!- SIMILARITY: Belongs to the UPF0051 (ycf24) family. {ECO:0000305}.
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DR EMBL; U00096; AAC74751.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15456.1; -; Genomic_DNA.
DR PIR; A64926; A64926.
DR RefSeq; NP_416196.1; NC_000913.3.
DR RefSeq; WP_000907979.1; NZ_SSZK01000001.1.
DR PDB; 1VH4; X-ray; 1.75 A; A/B=1-423.
DR PDB; 2ZU0; X-ray; 2.20 A; A/B=1-423.
DR PDB; 5AWF; X-ray; 2.96 A; B/F=1-423.
DR PDB; 5AWG; X-ray; 4.28 A; B/F=1-423.
DR PDBsum; 1VH4; -.
DR PDBsum; 2ZU0; -.
DR PDBsum; 5AWF; -.
DR PDBsum; 5AWG; -.
DR AlphaFoldDB; P77689; -.
DR SMR; P77689; -.
DR BioGRID; 4260280; 82.
DR BioGRID; 849278; 2.
DR ComplexPortal; CPX-2123; sufBCD complex.
DR DIP; DIP-10940N; -.
DR IntAct; P77689; 8.
DR MINT; P77689; -.
DR STRING; 511145.b1681; -.
DR jPOST; P77689; -.
DR PaxDb; P77689; -.
DR PRIDE; P77689; -.
DR EnsemblBacteria; AAC74751; AAC74751; b1681.
DR EnsemblBacteria; BAA15456; BAA15456; BAA15456.
DR GeneID; 944878; -.
DR KEGG; ecj:JW1671; -.
DR KEGG; eco:b1681; -.
DR PATRIC; fig|1411691.4.peg.577; -.
DR EchoBASE; EB3721; -.
DR eggNOG; COG0719; Bacteria.
DR HOGENOM; CLU_026231_5_0_6; -.
DR InParanoid; P77689; -.
DR OMA; PNCESHQ; -.
DR PhylomeDB; P77689; -.
DR BioCyc; EcoCyc:G6907-MON; -.
DR EvolutionaryTrace; P77689; -.
DR PRO; PR:P77689; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IDA:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR InterPro; IPR000825; SUF_FeS_clus_asmbl_SufBD.
DR InterPro; IPR037284; SUF_FeS_clus_asmbl_SufBD_sf.
DR InterPro; IPR011542; SUF_FeS_clus_asmbl_SufD.
DR PANTHER; PTHR43575; PTHR43575; 1.
DR Pfam; PF01458; SUFBD; 1.
DR SUPFAM; SSF101960; SSF101960; 1.
DR TIGRFAMs; TIGR01981; sufD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..423
FT /note="FeS cluster assembly protein SufD"
FT /id="PRO_0000147375"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:1VH4"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5AWF"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:5AWF"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:1VH4"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1VH4"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1VH4"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 166..177
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 182..195
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 197..207
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2ZU0"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 326..336
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5AWF"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:1VH4"
FT STRAND 354..365
FT /evidence="ECO:0007829|PDB:1VH4"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:1VH4"
FT HELIX 382..398
FT /evidence="ECO:0007829|PDB:1VH4"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:2ZU0"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:1VH4"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:2ZU0"
SQ SEQUENCE 423 AA; 46823 MW; 5744291F1E0AE825 CRC64;
MAGLPNSSNA LQQWHHLFEA EGTKRSPQAQ QHLQQLLRTG LPTRKHENWK YTPLEGLINS
QFVSIAGEIS PQQRDALALT LDSVRLVFVD GRYVPALSDA TEGSGYEVSI NDDRQGLPDA
IQAEVFLHLT ESLAQSVTHI AVKRGQRPAK PLLLMHITQG VAGEEVNTAH YRHHLDLAEG
AEATVIEHFV SLNDARHFTG ARFTINVAAN AHLQHIKLAF ENPLSHHFAH NDLLLAEDAT
AFSHSFLLGG AVLRHNTSTQ LNGENSTLRI NSLAMPVKNE VCDTRTWLEH NKGFCNSRQL
HKTIVSDKGR AVFNGLINVA QHAIKTDGQM TNNNLLMGKL AEVDTKPQLE IYADDVKCSH
GATVGRIDDE QIFYLRSRGI NQQDAQQMII YAFAAELTEA LRDEGLKQQV LARIGQRLPG
GAR
