ISCU_STRP1
ID ISCU_STRP1 Reviewed; 159 AA.
AC Q9A1G2; Q490V4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU;
DE AltName: Full=Sulfur acceptor protein IscU;
GN Name=iscU; Synonyms=nifU; OrderedLocusNames=M5005_Spy0245, SPy_0289;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ZINC, AND COFACTOR.
RC STRAIN=ATCC 12344 / CIP 56.41 / DSM 20565 / JCM 5674 / NCTC 8198;
RX PubMed=15815978; DOI=10.1002/prot.20421;
RA Liu J., Oganesyan N., Shin D.H., Jancarik J., Yokota H., Kim R., Kim S.H.;
RT "Structural characterization of an iron-sulfur cluster assembly protein
RT IscU in a zinc-bound form.";
RL Proteins 59:875-881(2005).
CC -!- FUNCTION: A scaffold on which IscS assembles Fe-S clusters.
CC Subsequently gives the nascent cluster to other proteins. It is likely
CC that Fe-S cluster coordination is flexible as the role of this complex
CC is to build and then hand off Fe-S clusters (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15815978};
CC Note=Binds 1 Zn(2+) ion; this is probably a substitute for Fe-S
CC centers. {ECO:0000269|PubMed:15815978};
CC -!- SUBUNIT: Forms a heterotetramer with IscS; each subunit of the IscS
CC dimer contacts an IscU monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR EMBL; AE004092; AAK33358.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ50864.1; -; Genomic_DNA.
DR RefSeq; NP_268637.1; NC_002737.2.
DR PDB; 1SU0; X-ray; 2.30 A; B=1-159.
DR PDBsum; 1SU0; -.
DR AlphaFoldDB; Q9A1G2; -.
DR SMR; Q9A1G2; -.
DR STRING; 1314.HKU360_00284; -.
DR PaxDb; Q9A1G2; -.
DR PRIDE; Q9A1G2; -.
DR EnsemblBacteria; AAK33358; AAK33358; SPy_0289.
DR KEGG; spy:SPy_0289; -.
DR KEGG; spz:M5005_Spy0245; -.
DR PATRIC; fig|160490.10.peg.253; -.
DR HOGENOM; CLU_079283_4_0_9; -.
DR OMA; MKLDSMY; -.
DR EvolutionaryTrace; Q9A1G2; -.
DR Proteomes; UP000000750; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
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; Zinc.
FT CHAIN 1..159
FT /note="Iron-sulfur cluster assembly scaffold protein IscU"
FT /id="PRO_0000428753"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15815978"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15815978"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15815978"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15815978"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:1SU0"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1SU0"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1SU0"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1SU0"
FT STRAND 43..63
FT /evidence="ECO:0007829|PDB:1SU0"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:1SU0"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:1SU0"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1SU0"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:1SU0"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:1SU0"
SQ SEQUENCE 159 AA; 17142 MW; 5233C0EF6A131211 CRC64;
MALSKLNHLY MAVVADHSKR PHHHGQLDGV EAVQLNNPTC GDVISLTVKF DEDKIEDIAF
AGNGCTISTA SSSMMTDAVI GKSKEEALAL ADIFSEMVQG QENPAQKELG EAELLAGVAK
FPQRIKCSTL AWNALKEAIK RSANAQHLTD QNVKEGKNV
