FIC_SALTY
ID FIC_SALTY Reviewed; 200 AA.
AC P20751;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable protein adenylyltransferase Fic;
DE EC=2.7.7.n1;
DE AltName: Full=Cell filamentation protein Fic;
GN Name=fic; OrderedLocusNames=STM3470;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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. {ECO:0000250}.
CC -!- FUNCTION: Involved in cell filamentation induced by cyclic AMP.
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 -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
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DR EMBL; M32355; AAA27176.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22332.1; -; Genomic_DNA.
DR RefSeq; NP_462373.1; NC_003197.2.
DR RefSeq; WP_001280671.1; NC_003197.2.
DR AlphaFoldDB; P20751; -.
DR SMR; P20751; -.
DR STRING; 99287.STM3470; -.
DR PaxDb; P20751; -.
DR EnsemblBacteria; AAL22332; AAL22332; STM3470.
DR GeneID; 1254993; -.
DR KEGG; stm:STM3470; -.
DR PATRIC; fig|99287.12.peg.3667; -.
DR HOGENOM; CLU_080158_0_5_6; -.
DR OMA; FCHFEYI; -.
DR PhylomeDB; P20751; -.
DR BioCyc; SENT99287:STM3470-MON; -.
DR Proteomes; UP000001014; 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; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..200
FT /note="Probable protein adenylyltransferase Fic"
FT /id="PRO_0000087241"
FT DOMAIN 54..191
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 CONFLICT 88
FT /note="R -> P (in Ref. 1; AAA27176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22781 MW; D83A6CEDD7BE4F65 CRC64;
MSDKFGEGRD PYLYPGLNVM RNRLGIHQAQ RLAQAAYEMT ALRAATIELG PLVRGLPHLC
AIHRQLYQDI FDWAGQLREV DIYQGDTRFC HFAYIEKEGN ALMQDLEEEG YLVGLAHEKF
VERLAHYYCE INVLHPFRFG SGLAQRIFFE QLALHAGYAL SWQGIAVETW KQANQSGAMG
DLSALRAIFQ KAISEARETE
