CYAA_HAEIN
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 03-AUG-2022, entry version 108.
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; Proteobacteria; 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}.
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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 RefSeq; WP_005694539.1; 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 OMA; YDDYVMS; -.
DR PhylomeDB; P40134; -.
DR BioCyc; HINF71421:G1GJ1-623-MON; -.
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; PTHR38760; 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
