ID   CYAA_ECOLI              Reviewed;         848 AA.
AC   P00936; Q2M8B1;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 5.
DT   02-SEP-2026, entry version 178.
DE   RecName: Full=Adenylate cyclase;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase;
DE   AltName: Full=Adenylyl cyclase;
GN   Name=cyaA; Synonyms=cya; OrderedLocusNames=b3806, JW3778;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6393056; DOI=10.1093/nar/12.24.9427;
RA   Aiba H., Mori K., Tanaka M., Ooi T., Roy A., Danchin A.;
RT   "The complete nucleotide sequence of the adenylate cyclase gene of
RT   Escherichia coli.";
RL   Nucleic Acids Res. 12:9427-9440(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=2982847; DOI=10.1016/s0021-9258(18)89473-x;
RA   Aiba H.;
RT   "Transcription of the Escherichia coli adenylate cyclase gene is negatively
RT   regulated by cAMP-cAMP receptor protein.";
RL   J. Biol. Chem. 260:3063-3070(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8874804; DOI=10.1016/0300-9084(96)82192-4;
RA   Trotot P., Sismeiro O., Vivares C., Glaser P., Bresson-Roy A., Danchin A.;
RT   "Comparative analysis of the cya locus in enterobacteria and related Gram-
RT   negative facultative anaerobes.";
RL   Biochimie 78:277-287(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=1379743; DOI=10.1126/science.1379743;
RA   Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT   84.5 to 86.5 minutes.";
RL   Science 257:771-778(1992).
RN   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-183.
RX   PubMed=6357786; DOI=10.1002/j.1460-2075.1983.tb01502.x;
RA   Roy A., Haziza C., Danchin A.;
RT   "Regulation of adenylate cyclase synthesis in Escherichia coli: nucleotide
RT   sequence of the control region.";
RL   EMBO J. 2:791-797(1983).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-88.
RX   PubMed=6344011; DOI=10.1093/nar/11.11.3451;
RA   Aiba H., Kawamukai M., Ishihama A.;
RT   "Cloning and promoter analysis of the Escherichia coli adenylate cyclase
RT   gene.";
RL   Nucleic Acids Res. 11:3451-3465(1983).
RN   [9]
RP   INDUCTION, REGULATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=19019153; DOI=10.1111/j.1365-2958.2008.06504.x;
RA   Iwamoto A., Lemire S., Yonesaki T.;
RT   "Post-transcriptional control of Crp-cAMP by RNase LS in Escherichia
RT   coli.";
RL   Mol. Microbiol. 70:1570-1578(2008).
RN   [10]
RP   REVIEW.
RX   PubMed=8418825;
RA   Danchin A.;
RT   "Phylogeny of adenylyl cyclases.";
RL   Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993).
CC   -!- FUNCTION: Catalyzes the formation of the second messenger cAMP from
CC       ATP. Its transcript is probably degraded by endoribonuclease LS (rnlA),
CC       decreasing cAMP levels and the negative regulator Crp-cAMP, which then
CC       induces its own transcription again.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC   -!- ACTIVITY REGULATION: The regulatory domain is involved in the
CC       regulation of cyclase activity by the carbon source. Activated by the
CC       PTS system, glucose-specific IIA component (CRR).
CC   -!- INTERACTION:
CC       P00936; P15038: helD; NbExp=3; IntAct=EBI-1116685, EBI-551473;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Repressed by the Crp-cAMP complex. Expression increases
CC       during growth, decreasing again in stationary phase; more strongly
CC       induced in an rnlA deletion mutant, levels remain high even in
CC       stationary phase (at protein level). {ECO:0000269|PubMed:19019153,
CC       ECO:0000269|PubMed:2982847}.
CC   -!- DISRUPTION PHENOTYPE: Not essential, eliminates the NaCl sensitivity of
CC       an rnlA deletion mutant. {ECO:0000269|PubMed:19019153}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Escherichia coli adenylate cyclase homepage;
CC       URL="http://minst.org/ecoli_cyclase.htm";
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DR   EMBL; X01653; CAA25817.1; -; Genomic_DNA.
DR   EMBL; X66782; CAA47280.1; -; Genomic_DNA.
DR   EMBL; M87049; AAA67602.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76809.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77495.1; -; Genomic_DNA.
DR   PIR; G65184; OYEC.
DR   RefSeq; NP_418250.1; NC_000913.3.
DR   RefSeq; WP_000281668.1; NZ_CP009789.1.
DR   AlphaFoldDB; P00936; -.
DR   BioGRID; 4262610; 24.
DR   BioGRID; 852067; 10.
DR   FunCoup; P00936; 168.
DR   IntAct; P00936; 23.
DR   STRING; 511145.b3806; -.
DR   jPOST; P00936; -.
DR   PaxDb; 511145-b3806; -.
DR   EnsemblBacteria; AAC76809; AAC76809; b3806.
DR   GeneID; 947755; -.
DR   KEGG; ecj:JW3778; -.
DR   KEGG; eco:b3806; -.
DR   KEGG; ecoc:C3026_20605; -.
DR   PATRIC; fig|1411691.4.peg.2902; -.
DR   EchoBASE; EB0168; -.
DR   eggNOG; COG3072; Bacteria.
DR   HOGENOM; CLU_013280_0_0_6; -.
DR   InParanoid; P00936; -.
DR   OMA; YDDYVMS; -.
DR   OrthoDB; 5571448at2; -.
DR   PhylomeDB; P00936; -.
DR   BioCyc; EcoCyc:ADENYLATECYC-MONOMER; -.
DR   BioCyc; MetaCyc:ADENYLATECYC-MONOMER; -.
DR   BRENDA; 4.6.1.1; 2026.
DR   PRO; PR:P00936; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P00936; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IDA:EcoCyc.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IMP:EcoCyc.
DR   InterPro; IPR060002; Adenylate_cycl_2nd.
DR   InterPro; IPR060066; Adenylate_cycl_3rd.
DR   InterPro; IPR060068; Adenylate_cycl_4th.
DR   InterPro; IPR060069; Adenylate_cycl_C.
DR   InterPro; IPR000274; Adenylate_cyclase_1.
DR   InterPro; IPR024686; Adenylate_cyclase_1_CS.
DR   InterPro; IPR024685; Adenylate_cyclase_1_N.
DR   NCBIfam; NF006977; PRK09450.1-1; 1.
DR   NCBIfam; NF006978; PRK09450.1-2; 1.
DR   NCBIfam; NF006979; PRK09450.1-4; 1.
DR   PANTHER; PTHR38760; ADENYLATE CYCLASE; 1.
DR   PANTHER; PTHR38760:SF1; ADENYLATE CYCLASE; 1.
DR   Pfam; PF12633; Adenyl_cycl_N; 1.
DR   Pfam; PF01295; Adenylate_cycl; 1.
DR   Pfam; PF26690; Adenylate_cycl_3rd; 1.
DR   Pfam; PF26691; Adenylate_cycl_4th; 1.
DR   Pfam; PF26693; Adenylate_cycl_C; 1.
DR   PIRSF; PIRSF001444; Adenylate_cycl; 1.
DR   PROSITE; PS01092; ADENYLATE_CYCLASE_1_1; 1.
DR   PROSITE; PS01093; ADENYLATE_CYCLASE_1_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; cAMP biosynthesis; Cytoplasm; Lyase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..848
FT                   /note="Adenylate cyclase"
FT                   /id="PRO_0000195669"
FT   REGION          1..535
FT                   /note="Catalytic"
FT   REGION          541..848
FT                   /note="Regulatory"
FT   MOD_RES         609
FT                   /note="Phosphohistidine; by CRR"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        223
FT                   /note="V -> G (in Ref. 1; CAA25817 and 3; CAA47280)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   848 AA;  97586 MW;  F0400E3406B15018 CRC64;
     MYLYIETLKQ RLDAINQLRV DRALAAMGPA FQQVYSLLPT LLHYHHPLMP GYLDGNVPKG
     ICLYTPDETQ RHYLNELELY RGMSVQDPPK GELPITGVYT MGSTSSVGQS CSSDLDIWVC
     HQSWLDSEER QLLQRKCSLL ENWAASLGVE VSFFLIDENR FRHNESGSLG GEDCGSTQHI
     LLLDEFYRTA VRLAGKRILW NMVPCDEEEH YDDYVMTLYA QGVLTPNEWL DLGGLSSLSA
     EEYFGASLWQ LYKSIDSPYK AVLKTLLLEA YSWEYPNPRL LAKDIKQRLH DGEIVSFGLD
     PYCMMLERVT EYLTAIEDFT RLDLVRRCFY LKVCEKLSRE RACVGWRRAV LSQLVSEWGW
     DEARLAMLDN RANWKIDQVR EAHNELLDAM MQSYRNLIRF ARRNNLSVSA SPQDIGVLTR
     KLYAAFEALP GKVTLVNPQI SPDLSEPNLT FIYVPPGRAN RSGWYLYNRA PNIESIISHQ
     PLEYNRYLNK LVAWAWFNGL LTSRTRLYIK GNGIVDLPKL QEMVADVSHH FPLRLPAPTP
     KALYSPCEIR HLAIIVNLEY DPTAAFRNQV VHFDFRKLDV FSFGENQNCL VGSVDLLYRN
     SWNEVRTLHF NGEQSMIEAL KTILGKMHQD AAPPDSVEVF CYSQHLRGLI RTRVQQLVSE
     CIELRLSSTR QETGRFKALR VSGQTWGLFF ERLNVSVQKL ENAIEFYGAI SHNKLHGLSV
     QVETNHVKLP AVVDGFASEG IIQFFFEETQ DENGFNIYIL DESNRVEVYH HCEGSKEELV
     RDVSRFYSSS HDRFTYGSSF INFNLPQFYQ IVKVDGREQV IPFRTKSIGN MPPANQDHDT
     PLLQQYFS
//