YDHX_ECOLI
ID YDHX_ECOLI Reviewed; 222 AA.
AC P77375;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 4.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Uncharacterized ferredoxin-like protein YdhX;
DE Flags: Precursor;
GN Name=ydhX; OrderedLocusNames=b1671, JW5271;
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=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(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 EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [5]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=18227264; DOI=10.1099/mic.0.2007/012146-0;
RA Partridge J.D., Browning D.F., Xu M., Newnham L.J., Scott C., Roberts R.E.,
RA Poole R.K., Green J.;
RT "Characterization of the Escherichia coli K-12 ydhYVWXUT operon: regulation
RT by FNR, NarL and NarP.";
RL Microbiology 154:608-618(2008).
CC -!- INDUCTION: Up-regulated by the oxygen-responsive transcription factor
CC FNR under anaerobic conditions. Repressed in the presence of nitrate or
CC nitrite via the two-component systems NarXL and NarPQ, respectively.
CC {ECO:0000269|PubMed:18227264}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven. Can also be exported by
CC the Sec system.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB47947.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC74741.4; -; Genomic_DNA.
DR EMBL; U68703; AAB47947.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP009048; BAA15443.2; -; Genomic_DNA.
DR PIR; G64924; G64924.
DR RefSeq; NP_416186.4; NC_000913.3.
DR RefSeq; WP_001310861.1; NZ_STEB01000003.1.
DR AlphaFoldDB; P77375; -.
DR SMR; P77375; -.
DR BioGRID; 4263343; 13.
DR DIP; DIP-48159N; -.
DR STRING; 511145.b1671; -.
DR PaxDb; P77375; -.
DR PRIDE; P77375; -.
DR EnsemblBacteria; AAC74741; AAC74741; b1671.
DR EnsemblBacteria; BAA15443; BAA15443; BAA15443.
DR GeneID; 66674436; -.
DR GeneID; 947308; -.
DR KEGG; ecj:JW5271; -.
DR KEGG; eco:b1671; -.
DR PATRIC; fig|1411691.4.peg.588; -.
DR EchoBASE; EB3716; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_1_3_6; -.
DR InParanoid; P77375; -.
DR OMA; EKCTWCY; -.
DR PhylomeDB; P77375; -.
DR BioCyc; EcoCyc:G6899-MON; -.
DR PRO; PR:P77375; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF13247; Fer4_11; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..27
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 28..222
FT /note="Uncharacterized ferredoxin-like protein YdhX"
FT /id="PRO_0000159295"
FT DOMAIN 37..67
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 83..114
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 115..144
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 222 AA; 25093 MW; 95FE1FC3687E6E0D CRC64;
MSFTRRKFVL GMGTVIFFTG SASSLLANTR QEKEVRYAMI HDESRCNGCN ICARACRKTN
HVPAQGSRLS IAHIPVTDND NETQYHFFRQ SCQHCEDAPC IDVCPTGASW RDEQGIVRVE
KSQCIGCSYC IGACPYQVRY LNPVTKVADK CDFCAESRLA KGFPPICVSA CPEHALIFGR
EDSPEIQAWL QQNKYYQYQL PGAGKPHLYR RFGQHLIKKE NV
