ID CYAA_HAEIN Reviewed; 843 AA. AC P40134; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 114. 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=HI_0604; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8226661; DOI=10.1128/jb.175.22.7142-7149.1993; RA Dorocicz I.R., Williams P.M., Redfield R.J.; RT "The Haemophilus influenzae adenylate cyclase gene: cloning, sequence, and RT essential role in competence."; RL J. Bacteriol. 175:7142-7149(1993). RN [2] 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). RN [3] RP INDUCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15769466; DOI=10.1016/j.jmb.2005.01.012; RA Redfield R.J., Cameron A.D., Qian Q., Hinds J., Ali T.R., Kroll J.S., RA Langford P.R.; RT "A novel CRP-dependent regulon controls expression of competence genes in RT Haemophilus influenzae."; RL J. Mol. Biol. 347:735-747(2005). CC -!- FUNCTION: Plays an essential role in competence development. 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. CC -!- INDUCTION: Expressed during exponential growth; expression decreases CC 10-fold on shifting to starvation media. {ECO:0000269|PubMed:15769466}. CC -!- DISRUPTION PHENOTYPE: Loss of competence, the ability to bind, take-up CC and integrate exogenous DNA. Loss of the ability to ferment ribose or CC xylose. {ECO:0000269|PubMed:8226661}. CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family. CC {ECO:0000305}. 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; L23824; AAC36855.1; -; Unassigned_DNA. DR EMBL; L42023; AAC22262.1; -; Genomic_DNA. DR PIR; A49922; A49922. DR RefSeq; NP_438762.1; NC_000907.1. DR AlphaFoldDB; P40134; -. DR STRING; 71421.HI_0604; -. DR EnsemblBacteria; AAC22262; AAC22262; HI_0604. DR KEGG; hin:HI_0604; -. DR PATRIC; fig|71421.8.peg.628; -. DR eggNOG; COG3072; Bacteria. DR HOGENOM; CLU_013280_0_0_6; -. DR OrthoDB; 5571448at2; -. DR PhylomeDB; P40134; -. DR BioCyc; HINF71421:G1GJ1-623-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0030420; P:establishment of competence for transformation; 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 2: Evidence at transcript level; KW ATP-binding; cAMP biosynthesis; Competence; Cytoplasm; Lyase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..843 FT /note="Adenylate cyclase" FT /id="PRO_0000195676" FT REGION 1..542 FT /note="Catalytic" FT /evidence="ECO:0000255" FT REGION 549..843 FT /note="Regulatory" FT /evidence="ECO:0000255" SQ SEQUENCE 843 AA; 97927 MW; B8C7BDFDFB07EEE7 CRC64; MECNLAQAKQ WVSALDQRRF ERALQGSGDA FQHVLAIVPL LLHLNHPQLP GYVIHAPSGI ASFLASDYQK KWLTNEYGIH YADHKPSTLK SAVNFHEVFP PILGVYVMGS FGSISQTSSS DLDTWICVRD GLSLDEYTLL TQKAKRISEW AMQFNVEINF YLMDQQRFRN EHYADPLTIE NSGSAQYMLL LDEFYRSAVR LAGKPLLWLH LWVENEKDYE KEVARLITEG EIDPNDWVDF GGLGQFSANE YFGASLWHLY KGIDSPYKSV LKILLLEAYS KEYPNTCLIA RTFKRDLLAG NTNPDHHFDP YIAILAKVTQ YLTALSEFKR LDFVHRCFYV KATEDFARYQ ANNWRIRYME ILAQEWGWSA ETVKHLNKRP FWKIKAVKEN HDNIMKFLML SYRNLVEFAR KHHIHSSVVP QDINILSRKL YTAFEELPGK VSLLNTQISH NLSEAHLTFV EVRGNKHFKD GWYLINQPIH HIMFSKERVI EYGESLNKLV SWAYFNHLLT EKTELSIFSK NVTLSTLQRF VTNLRQSFPS TIAKQPKNSD LLNQCEIRSL FIAINLTTDP TSKVEEVLTG ISSRDLFSFG SLEQSLVGSI DFTYRNVWNE IRTLHFEGQN AILLALKVLS NKIYRGVNRP DSIQVYCYSE RYRQDLRQLV MGLVNRCVSI QVGDIQQPCQ TSRLRVAGKN WQLFFEDRGI SLQEIGNESV CNEAESAVDF DEVLQTPIED GETNQESRRY PPEMDAFASE GFLQFFFEDN SDHSFNVYIL DESNHLEIYR HCDGEKDEKV REINQLYQNA KQEGDKNPYN IVQHNFNYPQ FYQLQNGKNG ISIVPFKFRQ MNK //