ID   CYAA_ECO57              Reviewed;         848 AA.
AC   Q8XAP1;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 105.
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; OrderedLocusNames=Z5322, ECs4736;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG58998.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38159.1; -; Genomic_DNA.
DR   PIR; B86067; B86067.
DR   PIR; H91220; H91220.
DR   RefSeq; NP_312763.1; NC_002695.1.
DR   RefSeq; WP_000281680.1; NZ_VOAI01000017.1.
DR   AlphaFoldDB; Q8XAP1; -.
DR   STRING; 155864.Z5322; -.
DR   GeneID; 66672290; -.
DR   GeneID; 915191; -.
DR   KEGG; ece:Z5322; -.
DR   KEGG; ecs:ECs_4736; -.
DR   PATRIC; fig|386585.9.peg.4942; -.
DR   eggNOG; COG3072; Bacteria.
DR   HOGENOM; CLU_013280_0_0_6; -.
DR   OMA; YDDYVMS; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000274; Adenylate_cyclase_1.
DR   InterPro; IPR024686; Adenylate_cyclase_1_CS.
DR   InterPro; IPR024685; Adenylate_cyclase_1_N.
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   PIRSF; PIRSF001444; Adenylate_cycl; 1.
DR   PROSITE; PS01092; ADENYLATE_CYCLASE_1_1; 1.
DR   PROSITE; PS01093; ADENYLATE_CYCLASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; cAMP biosynthesis; Cytoplasm; Lyase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..848
FT                   /note="Adenylate cyclase"
FT                   /id="PRO_0000195671"
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"
SQ   SEQUENCE   848 AA;  97559 MW;  BFEBE3547FBEE1C1 CRC64;
     MYLYIETLKQ RLDAINQLRV DRALAAMGPA FQQVYSLLPT LLHYHHPLMP GYLDGNVPKG
     ICLYTPDETQ RHYLNELELY RGMSVQDPPK GELPITGVYT MGSTSSVGQS CSSDLDIWVC
     HQSWLDSEER QLLQRKCSLL ESWAASLGVE 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
//