FDRA_ECOLI
ID FDRA_ECOLI Reviewed; 555 AA.
AC Q47208; Q2MBR0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein FdrA;
GN Name=fdrA; Synonyms=ylbD; OrderedLocusNames=b0518, JW0506;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7500942; DOI=10.1007/bf00290367;
RA Akiyama Y., Ito K.;
RT "A new Escherichia coli gene, fdrA, identified by suppression analysis of
RT dominant negative FtsH mutations.";
RL Mol. Gen. Genet. 249:202-208(1995).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-71.
RX PubMed=3309887; DOI=10.1093/nar/15.17.6827;
RA Mizuno T.;
RT "Random cloning of bent DNA segments from Escherichia coli chromosome and
RT primary characterization of their structures.";
RL Nucleic Acids Res. 15:6827-6841(1987).
CC -!- FUNCTION: Not known; multicopy suppressor of dominant negative ftsH
CC mutations.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: To E.coli YahF and some, to bacterial SucD. {ECO:0000305}.
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DR EMBL; D42020; BAA07638.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40270.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73620.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76296.1; -; Genomic_DNA.
DR EMBL; X05968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S60201; S60201.
DR RefSeq; NP_415051.1; NC_000913.3.
DR RefSeq; WP_000580829.1; NZ_LN832404.1.
DR PDB; 3DMY; X-ray; 2.07 A; A/B=82-555.
DR PDBsum; 3DMY; -.
DR AlphaFoldDB; Q47208; -.
DR SMR; Q47208; -.
DR BioGRID; 4261244; 129.
DR IntAct; Q47208; 3.
DR STRING; 511145.b0518; -.
DR PaxDb; Q47208; -.
DR PRIDE; Q47208; -.
DR EnsemblBacteria; AAC73620; AAC73620; b0518.
DR EnsemblBacteria; BAE76296; BAE76296; BAE76296.
DR GeneID; 946298; -.
DR KEGG; ecj:JW0506; -.
DR KEGG; eco:b0518; -.
DR PATRIC; fig|1411691.4.peg.1760; -.
DR EchoBASE; EB3180; -.
DR eggNOG; COG0074; Bacteria.
DR HOGENOM; CLU_026233_1_0_6; -.
DR OMA; KARRWES; -.
DR PhylomeDB; Q47208; -.
DR BioCyc; EcoCyc:G6287-MON; -.
DR EvolutionaryTrace; Q47208; -.
DR PRO; PR:Q47208; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.40.50.261; -; 2.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR SUPFAM; SSF52210; SSF52210; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..555
FT /note="Protein FdrA"
FT /id="PRO_0000087216"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3DMY"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:3DMY"
FT TURN 233..237
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 305..325
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 340..353
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:3DMY"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 410..418
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 427..440
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 449..456
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 464..473
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 482..492
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 519..527
FT /evidence="ECO:0007829|PDB:3DMY"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:3DMY"
FT HELIX 545..554
FT /evidence="ECO:0007829|PDB:3DMY"
SQ SEQUENCE 555 AA; 58596 MW; 732DBF9354E9297C CRC64;
MIHAFIKKGC FQDSVSLMII SRKLSESENV DDVSVMMGTP ANKALLDTTG FWHDDFNNAT
PNDICVAIRS EAADAGIAQA IMQQLEEALK QLAQGSGSSQ ALTQVRRWDS ACQKLPDANL
ALISVAGEYA AELANQALDR NLNVMMFSDN VTLEDEIQLK TRAREKGLLV MGPDCGTSMI
AGTPLAFANV MPEGNIGVIG ASGTGIQELC SQIALAGEGI THAIGLGGRD LSREVGGISA
LTALEMLSAD EKSEVLAFVS KPPAEAVRLK IVNAMKATGK PTVALFLGYT PAVARDENVW
FASSLDEAAR LACLLSRVTA RRNAIAPVSS GFICGLYTGG TLAAEAAGLL AGHLGVEADD
THQHGMMLDA DSHQIIDLGD DFYTVGRPHP MIDPTLRNQL IADLGAKPQV RVLLLDVVIG
FGATADPAAS LVSAWQKACA ARLDNQPLYA IATVTGTERD PQCRSQQIAT LEDAGIAVVS
SLPEATLLAA ALIHPLSPAA QQHTPSLLEN VAVINIGLRS FALELQSASK PVVHYQWSPV
AGGNKKLARL LERLQ
