FIC_ECOLI
ID FIC_ECOLI Reviewed; 200 AA.
AC P20605; Q2M727;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable protein adenylyltransferase Fic;
DE EC=2.7.7.n1;
DE AltName: Full=Cell filamentation protein Fic;
GN Name=fic; OrderedLocusNames=b3361, JW3324;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-55.
RX PubMed=2546924; DOI=10.1128/jb.171.8.4525-4529.1989;
RA Kawamukai M., Matsuda H., Fujii W., Utsumi R., Komano T.;
RT "Nucleotide sequences of fic and fic-1 genes involved in cell filamentation
RT induced by cyclic AMP in Escherichia coli.";
RL J. Bacteriol. 171:4525-4529(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2403545; DOI=10.1128/jb.172.1.397-410.1990;
RA Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P.;
RT "Chromosomal organization and expression of Escherichia coli pabA.";
RL J. Bacteriol. 172:397-410(1990).
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 1-18.
RX PubMed=7549107; DOI=10.1271/bbb.59.1573;
RA Utsumi R., Nakayama T., Iwamoto N., Kohda K., Kawamukai M., Tanabe H.,
RA Tanaka K., Takahashi H., Noda M.;
RT "Mutational analysis of the fic promoter recognized by RpoS (sigma 38) in
RT Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 59:1573-1575(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX PubMed=2007139; DOI=10.1021/bi00226a009;
RA Hayano T., Takahashi N., Kato S., Maki N., Suzuki M.;
RT "Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed
RT separately in periplasmic and cytoplasmic compartments of Escherichia coli
RT cells.";
RL Biochemistry 30:3041-3048(1991).
CC -!- FUNCTION: Probable adenylyltransferase that mediates the addition of
CC adenosine 5'-monophosphate (AMP) to specific residues of target
CC proteins (By similarity). Involved in cell filamentation induced by
CC cyclic AMP. May have some role in cell division. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1;
CC -!- INTERACTION:
CC P20605; P06710: dnaX; NbExp=2; IntAct=EBI-1132602, EBI-549140;
CC -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
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DR EMBL; M28363; AAA23773.1; -; Genomic_DNA.
DR EMBL; M32354; AAA24263.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58158.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76386.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77929.1; -; Genomic_DNA.
DR EMBL; S79599; AAB35351.1; -; Genomic_DNA.
DR EMBL; M55429; AAA23452.1; -; Genomic_DNA.
DR PIR; D65130; D65130.
DR RefSeq; NP_417820.1; NC_000913.3.
DR RefSeq; WP_001280641.1; NZ_SSZK01000008.1.
DR PDB; 5JFF; X-ray; 2.00 A; A/C=1-200.
DR PDB; 5JFZ; X-ray; 2.40 A; A/C/E=3-200.
DR PDBsum; 5JFF; -.
DR PDBsum; 5JFZ; -.
DR AlphaFoldDB; P20605; -.
DR SMR; P20605; -.
DR BioGRID; 4261083; 86.
DR BioGRID; 852183; 5.
DR DIP; DIP-9608N; -.
DR IntAct; P20605; 5.
DR STRING; 511145.b3361; -.
DR jPOST; P20605; -.
DR PaxDb; P20605; -.
DR PRIDE; P20605; -.
DR EnsemblBacteria; AAC76386; AAC76386; b3361.
DR EnsemblBacteria; BAE77929; BAE77929; BAE77929.
DR GeneID; 66672758; -.
DR GeneID; 947872; -.
DR KEGG; ecj:JW3324; -.
DR KEGG; eco:b3361; -.
DR PATRIC; fig|1411691.4.peg.3369; -.
DR EchoBASE; EB0303; -.
DR eggNOG; COG2184; Bacteria.
DR HOGENOM; CLU_080158_0_2_6; -.
DR InParanoid; P20605; -.
DR OMA; FCHFEYI; -.
DR PhylomeDB; P20605; -.
DR BioCyc; EcoCyc:EG10307-MON; -.
DR PRO; PR:P20605; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051302; P:regulation of cell division; IMP:EcoCyc.
DR Gene3D; 1.10.3290.10; -; 1.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR Pfam; PF02661; Fic; 1.
DR SUPFAM; SSF140931; SSF140931; 1.
DR PROSITE; PS51459; FIDO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..200
FT /note="Probable protein adenylyltransferase Fic"
FT /id="PRO_0000087240"
FT DOMAIN 54..195
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT BINDING 84..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 140..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 55
FT /note="G->R: Inhibitory effect on cell division induced by
FT cAMP with temperature sensitivity."
FT /evidence="ECO:0000269|PubMed:2546924"
FT CONFLICT 53..54
FT /note="VR -> GA (in Ref. 1; AAA23773)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="Missing (in Ref. 2; AAA24263)"
FT /evidence="ECO:0000305"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:5JFZ"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:5JFF"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:5JFF"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5JFF"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:5JFF"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:5JFF"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:5JFF"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5JFF"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:5JFF"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5JFF"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:5JFF"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5JFF"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:5JFF"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:5JFF"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5JFF"
SQ SEQUENCE 200 AA; 22960 MW; 3E7E0B034BEBC70C CRC64;
MSDKFGEGRD PYLYPGLDIM RNRLNIRQQQ RLEQAAYEMT ALRAATIELG PLVRGLPHLR
TIHRQLYQDI FDWAGQLREV DIYQGDTPFC HFAYIEKEGN ALMQDLEEEG YLVGLEKAKF
VERLAHYYCE INVLHPFRVG SGLAQRIFFE QLAIHAGYQL SWQGIEKEAW NQANQSGAMG
DLTALQMIFS KVVSEAGESE
