ID   B7MH67_ECO45            Unreviewed;       848 AA.
AC   B7MH67;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   04-NOV-2026, entry version 64.
DE   RecName: Full=Adenylate cyclase {ECO:0000256|ARBA:ARBA00021420, ECO:0000256|RuleBase:RU000604};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201, ECO:0000256|RuleBase:RU000604};
GN   Name=cyaA {ECO:0000313|EMBL:CAR05421.1};
GN   OrderedLocusNames=ECS88_4229 {ECO:0000313|EMBL:CAR05421.1};
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR05421.1, ECO:0000313|Proteomes:UP000000747};
RN   [1] {ECO:0000313|Proteomes:UP000000747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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         Evidence={ECO:0000256|ARBA:ARBA00001593,
CC         ECO:0000256|RuleBase:RU000604};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU000604}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC       {ECO:0000256|ARBA:ARBA00007901, ECO:0000256|RuleBase:RU004184}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU928161; CAR05421.1; -; Genomic_DNA.
DR   RefSeq; WP_000281691.1; NC_011742.1.
DR   AlphaFoldDB; B7MH67; -.
DR   KEGG; ecz:ECS88_4229; -.
DR   HOGENOM; CLU_013280_0_0_6; -.
DR   OMA; AAEWQWQ; -.
DR   Proteomes; UP000000747; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:InterPro.
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; cyaA; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998,
KW   ECO:0000256|RuleBase:RU000604}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000604};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000747}.
FT   DOMAIN          5..200
FT                   /note="Adenylate cyclase class-I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12633"
FT   DOMAIN          238..437
FT                   /note="Adenylate cyclase class-I second"
FT                   /evidence="ECO:0000259|Pfam:PF01295"
FT   DOMAIN          444..533
FT                   /note="Adenylate cyclase class-I third"
FT                   /evidence="ECO:0000259|Pfam:PF26690"
FT   DOMAIN          538..715
FT                   /note="Adenylate cyclase class-I fourth"
FT                   /evidence="ECO:0000259|Pfam:PF26691"
FT   DOMAIN          733..826
FT                   /note="Adenylate cyclase class-I C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF26693"
SQ   SEQUENCE   848 AA;  97700 MW;  469AB04FCB86E18B 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 RACVGWRREV LSQLVKEWEW
     DDARLAMLDN 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 MPPANQEHDA
     PLLQQYFS
//