SUFU_BACSU
ID SUFU_BACSU Reviewed; 147 AA.
AC O32163;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Zinc-dependent sulfurtransferase SufU;
DE EC=2.-.-.-;
DE AltName: Full=Putative iron-sulfur cluster assembly scaffold protein SufU;
DE AltName: Full=Sulfur acceptor protein SufU;
GN Name=sufU; Synonyms=iscU, nifU, yurV; OrderedLocusNames=BSU32680;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-128.
RC STRAIN=168 / PS832;
RX PubMed=20822158; DOI=10.1021/bi101358k;
RA Selbach B., Earles E., Dos Santos P.C.;
RT "Kinetic analysis of the bisubstrate cysteine desulfurase SufS from
RT Bacillus subtilis.";
RL Biochemistry 49:8794-8802(2010).
RN [3]
RP FUNCTION, BINDS AN FE-S CLUSTER, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASP-43.
RC STRAIN=168;
RX PubMed=20097860; DOI=10.1128/jb.01536-09;
RA Albrecht A.G., Netz D.J., Miethke M., Pierik A.J., Burghaus O.,
RA Peuckert F., Lill R., Marahiel M.A.;
RT "SufU is an essential iron-sulfur cluster scaffold protein in Bacillus
RT subtilis.";
RL J. Bacteriol. 192:1643-1651(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 21332 / IAM 1213;
RX PubMed=21744456; DOI=10.1002/cbic.201100190;
RA Albrecht A.G., Landmann H., Nette D., Burghaus O., Peuckert F., Seubert A.,
RA Miethke M., Marahiel M.A.;
RT "The frataxin homologue Fra plays a key role in intracellular iron
RT channeling in Bacillus subtilis.";
RL ChemBioChem 12:2052-2061(2011).
RN [5]
RP BINDS AN FE-S CLUSTER, INTERACTION WITH SUFS, SUBUNIT, AND MUTAGENESIS OF
RP CYS-41; CYS-66 AND CYS-128.
RC STRAIN=168;
RX PubMed=21236255; DOI=10.1016/j.febslet.2011.01.005;
RA Albrecht A.G., Peuckert F., Landmann H., Miethke M., Seubert A.,
RA Marahiel M.A.;
RT "Mechanistic characterization of sulfur transfer from cysteine desulfurase
RT SufS to the iron-sulfur scaffold SufU in Bacillus subtilis.";
RL FEBS Lett. 585:465-470(2011).
RN [6]
RP FUNCTION AS A SULFURTRANSFERASE, ZINC-BINDING, COFACTOR, AND MUTAGENESIS OF
RP CYS-41; ASP-43; CYS-66 AND CYS-128.
RC STRAIN=168 / PS832;
RX PubMed=24321018; DOI=10.1021/bi4011978;
RA Selbach B.P., Chung A.H., Scott A.D., George S.J., Cramer S.P.,
RA Dos Santos P.C.;
RT "Fe-S cluster biogenesis in Gram-positive bacteria: SufU is a zinc-
RT dependent sulfur transfer protein.";
RL Biochemistry 53:152-160(2014).
RN [7]
RP FUNCTION, AND INTERACTION WITH FRA AND SUFS.
RX PubMed=27382962; DOI=10.1371/journal.pone.0158749;
RA Blauenburg B., Mielcarek A., Altegoer F., Fage C.D., Linne U., Bange G.,
RA Marahiel M.A.;
RT "Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its
RT Dynamic Interaction with Frataxin and Scaffold Protein SufU.";
RL PLoS ONE 11:e0158749-e0158749(2016).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-41; CYS-66 AND
RP CYS-128.
RC STRAIN=168;
RX PubMed=29292548; DOI=10.1111/mmi.13907;
RA Yokoyama N., Nonaka C., Ohashi Y., Shioda M., Terahata T., Chen W.,
RA Sakamoto K., Maruyama C., Saito T., Yuda E., Tanaka N., Fujishiro T.,
RA Kuzuyama T., Asai K., Takahashi Y.;
RT "Distinct roles for U-type proteins in iron-sulfur cluster biosynthesis
RT revealed by genetic analysis of the Bacillus subtilis sufCDSUB operon.";
RL Mol. Microbiol. 107:688-703(2018).
RN [9]
RP STRUCTURE BY NMR IN COMPLEX WITH ZINC.
RA Kornhaber G.J., Swapna G.V.T., Ramelot T.A., Cort J.R., Kennedy M.A.,
RA Montelione G.T.;
RT "Solution structure of iron-sulfur cluster assembly protein IscU from
RT Bacillus subtilis, with zinc bound at the active site. Northeast Structural
RT Genomics Consortium Target SR17.";
RL Submitted (SEP-2004) to the PDB data bank.
RN [10]
RP STRUCTURE BY NMR IN COMPLEX WITH ZINC.
RA Kornhaber G.J., Swapna G.V.T., Ramelot T.A., Cort J.R., Aramini J.M.,
RA Kennedy M.A., Montelione G.T.;
RT "Solution NMR structure of Zn-ligated Fe-S cluster assembly scaffold
RT protein SufU From Bacillus subtilis.";
RL Submitted (SEP-2005) to the PDB data bank.
RN [11] {ECO:0007744|PDB:5XT5, ECO:0007744|PDB:5XT6}
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION,
RP INTERACTION WITH SUFS, AND ACTIVITY REGULATION.
RC STRAIN=168;
RX PubMed=29235855; DOI=10.1021/jacs.7b11307;
RA Fujishiro T., Terahata T., Kunichika K., Yokoyama N., Maruyama C., Asai K.,
RA Takahashi Y.;
RT "Zinc-Ligand Swapping Mediated Complex Formation and Sulfur Transfer
RT between SufS and SufU for Iron-Sulfur Cluster Biogenesis in Bacillus
RT subtilis.";
RL J. Am. Chem. Soc. 139:18464-18467(2017).
CC -!- FUNCTION: Part of the SUF-like system that mediates the biosynthesis of
CC iron-sulfur (Fe-S) clusters. Acts as a sulfurtransferase and thus
CC transfers sulfur from SufS to SufB (PubMed:29292548). Mechanistically,
CC the transfer from SufS to SufU is triggered by zinc-ligand swapping
CC that provides a free thiol from SufU to accept sulfur from SufS
CC (PubMed:29235855). {ECO:0000269|PubMed:20097860,
CC ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255,
CC ECO:0000269|PubMed:21744456, ECO:0000269|PubMed:24321018,
CC ECO:0000269|PubMed:27382962, ECO:0000269|PubMed:29235855,
CC ECO:0000269|PubMed:29292548}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24321018};
CC Note=Bind 1 Zn(2+) per monomer. {ECO:0000269|PubMed:24321018};
CC -!- SUBUNIT: Interacts with SufS; this interaction enhances SufS cysteine
CC desulfurase activity. Interacts with frataxin/Fra (PubMed:27382962).
CC {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255,
CC ECO:0000269|PubMed:27382962}.
CC -!- INTERACTION:
CC O32163; O32164: sufS; NbExp=8; IntAct=EBI-8561343, EBI-7826704;
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted. Upon depletion
CC cells grow very slowly while aconitase and succinate dehydrogenase,
CC both of which contain Fe-S clusters, have decreased activity. Upon
CC depletion no change in reactive oxygen species is observed, while a
CC modified bacillibactin (BB), an endogenous siderophore, is produced.
CC {ECO:0000269|PubMed:20097860, ECO:0000269|PubMed:21744456,
CC ECO:0000269|PubMed:29292548}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an iron-sulfur cluster assembly
CC scaffold protein (PubMed:20097860, PubMed:21236255). It is now thought
CC to be a zinc-dependent sulfur transfer protein (PubMed:24321018).
CC {ECO:0000305|PubMed:20097860, ECO:0000305|PubMed:21236255,
CC ECO:0000305|PubMed:24321018}.
CC -!- CAUTION: The inhibition of SufS activity by the Cys-41 mutation in this
CC protein has been described as competitive and non-competitive
CC inhibition (PubMed:21236255, PubMed:24321018).
CC {ECO:0000305|PubMed:21236255, ECO:0000305|PubMed:24321018}.
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DR EMBL; AL009126; CAB15257.1; -; Genomic_DNA.
DR PIR; E70019; E70019.
DR RefSeq; NP_391147.1; NC_000964.3.
DR RefSeq; WP_003222809.1; NZ_JNCM01000033.1.
DR PDB; 1XJS; NMR; -; A=1-147.
DR PDB; 2AZH; NMR; -; A=1-147.
DR PDB; 5XT5; X-ray; 2.34 A; C/D=1-147.
DR PDB; 5XT6; X-ray; 3.50 A; C/D=1-147.
DR PDB; 6JZV; X-ray; 2.00 A; A/B/C/D=1-147.
DR PDB; 6JZW; X-ray; 2.64 A; A/B/C/D=1-147.
DR PDBsum; 1XJS; -.
DR PDBsum; 2AZH; -.
DR PDBsum; 5XT5; -.
DR PDBsum; 5XT6; -.
DR PDBsum; 6JZV; -.
DR PDBsum; 6JZW; -.
DR AlphaFoldDB; O32163; -.
DR BMRB; O32163; -.
DR SMR; O32163; -.
DR IntAct; O32163; 1.
DR MINT; O32163; -.
DR STRING; 224308.BSU32680; -.
DR jPOST; O32163; -.
DR PaxDb; O32163; -.
DR PRIDE; O32163; -.
DR EnsemblBacteria; CAB15257; CAB15257; BSU_32680.
DR GeneID; 50136190; -.
DR GeneID; 64305023; -.
DR GeneID; 936702; -.
DR KEGG; bsu:BSU32680; -.
DR PATRIC; fig|224308.179.peg.3539; -.
DR eggNOG; COG0822; Bacteria.
DR InParanoid; O32163; -.
DR OMA; MKLDSMY; -.
DR PhylomeDB; O32163; -.
DR BioCyc; BSUB:BSU32680-MON; -.
DR EvolutionaryTrace; O32163; -.
DR PRO; PR:O32163; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR CDD; cd06664; IscU_like; 1.
DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR PANTHER; PTHR10093; PTHR10093; 1.
DR Pfam; PF01592; NifU_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..147
FT /note="Zinc-dependent sulfurtransferase SufU"
FT /id="PRO_0000166180"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29235855, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.9"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29235855, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.9"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29235855, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.9"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29235855, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.9"
FT MUTAGEN 41
FT /note="C->A: Does not activate SufS; dominant negative to
FT wild-type protein, interacts with SufS. Binds about 40%
FT Zn(2+)."
FT /evidence="ECO:0000269|PubMed:21236255,
FT ECO:0000269|PubMed:24321018"
FT MUTAGEN 41
FT /note="C->D: Complete loss of growth without mevalonate."
FT /evidence="ECO:0000269|PubMed:29292548"
FT MUTAGEN 43
FT /note="D->A: Increases stability of the bound Fe-S cluster.
FT Binds SufS, binds about 35% Zn(2+)."
FT /evidence="ECO:0000269|PubMed:20097860,
FT ECO:0000269|PubMed:24321018"
FT MUTAGEN 66
FT /note="C->A: Does not interact with SufS, does not activate
FT SufS; no effect in presence of wild-type protein. Binds
FT about 15% Zn(2+)."
FT /evidence="ECO:0000269|PubMed:21236255,
FT ECO:0000269|PubMed:24321018"
FT MUTAGEN 66
FT /note="C->D: Complete loss of growth without mevalonate."
FT /evidence="ECO:0000269|PubMed:29292548"
FT MUTAGEN 128
FT /note="C->A: Does not interact with SufS, does not activate
FT SufS; no effect in presence of wild-type protein. Binds
FT about 45% Zn(2+)."
FT /evidence="ECO:0000269|PubMed:20822158,
FT ECO:0000269|PubMed:21236255, ECO:0000269|PubMed:24321018"
FT MUTAGEN 128
FT /note="C->D: Delayed growth without mevalonate."
FT /evidence="ECO:0000269|PubMed:29292548"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:6JZV"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6JZV"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:6JZV"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:6JZV"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:6JZV"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:6JZV"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:6JZV"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:6JZV"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:6JZV"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6JZV"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:6JZV"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2AZH"
SQ SEQUENCE 147 AA; 16166 MW; 03F8195352E64EE2 CRC64;
MSFNANLDTL YRQVIMDHYK NPRNKGVLND SIVVDMNNPT CGDRIRLTMK LDGDIVEDAK
FEGEGCSISM ASASMMTQAI KGKDIETALS MSKIFSDMMQ GKEYDDSIDL GDIEALQGVS
KFPARIKCAT LSWKALEKGV AKEEGGN
