ID   Y977_HAEIN              Reviewed;         191 AA.
AC   P44088;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Probable protein adenylyltransferase HI_0977;
DE            EC=2.7.7.n1;
GN   OrderedLocusNames=HI_0977;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Probable adenylyltransferase that mediates the addition of
CC       adenosine 5'-monophosphate (AMP) to specific residues of target
CC       proteins. {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   -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22637.1; -; Genomic_DNA.
DR   PIR; G64017; G64017.
DR   RefSeq; NP_439140.1; NC_000907.1.
DR   RefSeq; WP_005690872.1; NC_000907.1.
DR   AlphaFoldDB; P44088; -.
DR   SMR; P44088; -.
DR   STRING; 71421.HI_0977; -.
DR   DNASU; 949973; -.
DR   EnsemblBacteria; AAC22637; AAC22637; HI_0977.
DR   KEGG; hin:HI_0977; -.
DR   PATRIC; fig|71421.8.peg.1020; -.
DR   eggNOG; COG2184; Bacteria.
DR   HOGENOM; CLU_080158_4_0_6; -.
DR   OMA; GHFRFAN; -.
DR   PhylomeDB; P44088; -.
DR   BioCyc; HINF71421:G1GJ1-1019-MON; -.
DR   Proteomes; UP000000579; 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..191
FT                   /note="Probable protein adenylyltransferase HI_0977"
FT                   /id="PRO_0000077987"
FT   DOMAIN          37..162
FT                   /note="Fido"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT   BINDING         67..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         112..114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   191 AA;  22541 MW;  5C327D09F6D2E93E CRC64;
     MPPKFWIIII VKKIDQQSLE NAYRLFESGD IHQIEIGSTK GLQQIHHYLF NGLYEFAGKI
     REQNISKGHF RFANALYLKE ALGKIEQMPE DTFENIINKY VEMNIAHPFL EGNGRSTRIW
     LDLVLKKHLG KVVNWQNVDK TQYLQAMERS PINDLEIRFL LQANLTDDVN NREIIFKGIE
     QSYYYEGYEK E