ERPA_ECOLI
ID ERPA_ECOLI Reviewed; 114 AA.
AC P0ACC3; P37026;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Iron-sulfur cluster insertion protein ErpA;
GN Name=erpA; Synonyms=yadR; OrderedLocusNames=b0156, JW0152;
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=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP CHARACTERIZATION, DISRUPTION PHENOTYPE, COFACTOR, AND MUTAGENESIS OF
RP CYS-42; CYS-106 AND CYS-108.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17698959; DOI=10.1073/pnas.0705829104;
RA Loiseau L., Gerez C., Bekker M., Ollagnier-de Choudens S., Py B.,
RA Sanakis Y., Teixeira de Mattos J., Fontecave M., Barras F.;
RT "ErpA, an iron sulfur (Fe S) protein of the A-type essential for
RT respiratory metabolism in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13626-13631(2007).
CC -!- FUNCTION: Probably involved in the insertion of Fe-S clusters into
CC apoproteins in vivo including IspG and/or IspH. Essential for growth
CC under aerobic conditions and for anaerobic respiration but not for
CC fermentation. In vitro it binds Fe-S clusters and transfers them to
CC apo-IspG, which is involved in quinone biosynthesis among many other
CC cell components. Experiments indicate that it is probably also involved
CC in the insertion of other Fe-S clusters than IspG/IspH.
CC -!- COFACTOR:
CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC Evidence={ECO:0000269|PubMed:17698959};
CC Note=Binds 1 iron-sulfur cluster per subunit. A study found 40-50% as
CC [2Fe-2S] clusters, 15-25% as [4Fe-4S] clusters and the rest as
CC paramagnetic iron. {ECO:0000269|PubMed:17698959};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Reduced amounts of quinones.
CC {ECO:0000269|PubMed:17698959}.
CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
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DR EMBL; U70214; AAB08586.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73267.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96733.1; -; Genomic_DNA.
DR PIR; S45225; S45225.
DR RefSeq; NP_414698.1; NC_000913.3.
DR RefSeq; WP_001295564.1; NZ_STEB01000032.1.
DR AlphaFoldDB; P0ACC3; -.
DR SMR; P0ACC3; -.
DR BioGRID; 4261657; 299.
DR DIP; DIP-48196N; -.
DR IntAct; P0ACC3; 8.
DR STRING; 511145.b0156; -.
DR ChEMBL; CHEMBL3309017; -.
DR jPOST; P0ACC3; -.
DR PaxDb; P0ACC3; -.
DR PRIDE; P0ACC3; -.
DR EnsemblBacteria; AAC73267; AAC73267; b0156.
DR EnsemblBacteria; BAB96733; BAB96733; BAB96733.
DR GeneID; 67416233; -.
DR GeneID; 944857; -.
DR KEGG; ecj:JW0152; -.
DR KEGG; eco:b0156; -.
DR PATRIC; fig|1411691.4.peg.2124; -.
DR EchoBASE; EB2236; -.
DR eggNOG; COG0316; Bacteria.
DR HOGENOM; CLU_069054_5_3_6; -.
DR InParanoid; P0ACC3; -.
DR OMA; YQLYFDE; -.
DR PhylomeDB; P0ACC3; -.
DR BioCyc; EcoCyc:EG12332-MON; -.
DR PRO; PR:P0ACC3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoCyc.
DR GO; GO:0051604; P:protein maturation; IDA:EcoCyc.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IBA:GO_Central.
DR Gene3D; 2.60.300.12; -; 1.
DR HAMAP; MF_01380; Fe_S_insert_ErpA; 1.
DR InterPro; IPR000361; FeS_biogenesis.
DR InterPro; IPR016092; FeS_cluster_insertion.
DR InterPro; IPR017870; FeS_cluster_insertion_CS.
DR InterPro; IPR023063; FeS_cluster_insertion_RrpA.
DR InterPro; IPR035903; HesB-like_dom_sf.
DR Pfam; PF01521; Fe-S_biosyn; 1.
DR SUPFAM; SSF89360; SSF89360; 1.
DR TIGRFAMs; TIGR00049; TIGR00049; 1.
DR PROSITE; PS01152; HESB; 1.
PE 1: Evidence at protein level;
KW Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..114
FT /note="Iron-sulfur cluster insertion protein ErpA"
FT /id="PRO_0000076990"
FT BINDING 42
FT /ligand="iron-sulfur cluster"
FT /ligand_id="ChEBI:CHEBI:30408"
FT /evidence="ECO:0000305"
FT BINDING 106
FT /ligand="iron-sulfur cluster"
FT /ligand_id="ChEBI:CHEBI:30408"
FT /evidence="ECO:0000305"
FT BINDING 108
FT /ligand="iron-sulfur cluster"
FT /ligand_id="ChEBI:CHEBI:30408"
FT /evidence="ECO:0000305"
FT MUTAGEN 42
FT /note="C->S: Does not complement knockout."
FT /evidence="ECO:0000269|PubMed:17698959"
FT MUTAGEN 106
FT /note="C->S: Does not complement knockout."
FT /evidence="ECO:0000269|PubMed:17698959"
FT MUTAGEN 108
FT /note="C->S: Does not complement knockout."
FT /evidence="ECO:0000269|PubMed:17698959"
SQ SEQUENCE 114 AA; 12100 MW; 5A032FB5C3E0D04A CRC64;
MSDDVALPLE FTDAAANKVK SLIADEDNPN LKLRVYITGG GCSGFQYGFT FDDQVNEGDM
TIEKQGVGLV VDPMSLQYLV GGSVDYTEGL EGSRFIVTNP NAKSTCGCGS SFSI
