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Database: UniProt
Entry: A0A0Q4XJ07_9BURK
LinkDB: A0A0Q4XJ07_9BURK
Original site: A0A0Q4XJ07_9BURK 
ID   A0A0Q4XJ07_9BURK        Unreviewed;       979 AA.
AC   A0A0Q4XJ07;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Diguanylate cyclase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASF43_23925 {ECO:0000313|EMBL:KQP11993.1};
OS   Pseudorhodoferax sp. Leaf267.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP11993.1, ECO:0000313|Proteomes:UP000051560};
RN   [1] {ECO:0000313|EMBL:KQP11993.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP11993.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP11993.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP11993.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQP11993.1}.
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DR   EMBL; LMMV01000027; KQP11993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4XJ07; -.
DR   STRING; 1736316.ASF43_23925; -.
DR   Proteomes; UP000051560; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd01948; EAL; 1.
DR   CDD; cd01949; GGDEF; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.20.20.450; EAL domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001633; EAL_dom.
DR   InterPro; IPR035919; EAL_sf.
DR   InterPro; IPR000160; GGDEF_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR021796; Tll0287-like.
DR   NCBIfam; TIGR00254; GGDEF; 1.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR44757:SF2; BIOFILM ARCHITECTURE MAINTENANCE PROTEIN MBAA; 1.
DR   PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR   Pfam; PF11845; DUF3365; 1.
DR   Pfam; PF00563; EAL; 1.
DR   Pfam; PF00990; GGDEF; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00052; EAL; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF141868; EAL domain-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50883; EAL; 1.
DR   PROSITE; PS50887; GGDEF; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051560};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          297..327
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          353..407
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          439..571
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   DOMAIN          580..834
FT                   /note="EAL"
FT                   /evidence="ECO:0000259|PROSITE:PS50883"
FT   DOMAIN          849..964
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         898
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   979 AA;  108002 MW;  A540BA382F77B382 CRC64;
     MVILTGVFAL ACGLGYLVVR DAVNKTVEHQ ALSIAKVVAS QAAELRSVYA QRIAGQLQPD
     GTLARDPATG QASLPPHFMT FSGPGAAAAE DQLFEFTPVS PWNLEPARGL NDDFLRWAWP
     QLERQNQAAP TGPITWTAVS RIEEQGGRRV LRYLAADPAS QPACIACHNA YERTPAVMAL
     RTASGLAPVQ PFALHQLMGG LSVTIPLDES QAVAGRQIRQ ATVFFFAILL ASFVAMVWFN
     WRIGLQRTSL RRAKLELARV ALDARSANER LNAQQGVEQA FAELSTYMRG IDQHALVSVT
     DRSGRIVQVN DKFVAISGYR REALLGQDHR IVNSNAHSRA FFSKMWETIG RGEIWRDVIC
     NRANEGALYW VDAAIVPLKD AAGEVVRYIA VCVDITEQRR HEDALHYQAT HDGLTDLPNR
     VLLLDRVGQA IAQARREQHE VVLFFIDLDK FKQINDSLGH SAGDKVLCEM ARRLVALARG
     GDTVARLGGD EFVVACAGLG RADVQAMGAR ISQALNAPVK LGGEHHTLGG SVGVAVYPEH
     GQDTETLLKR ADIAMYQAKG RGGSGVCFFS PEMQDAIDVR VQMESRLREG IEREELVLHY
     QPQVDFETGT LVSLEALLRW DSPHYGFLMP GQFIGLAEES KLIDALDAFV LNAACRQMQH
     WHRKGYGWIR TAVNLAATKF SDPGFKAELT STMARYGIPA GYLELEVTES LSMRDPNAAL
     ELMRDLKSAG ILLAIDDFGT GYSNLGYLKR FPADRLKVDQ SFVRGLMKNP QDRAIVAAVI
     QLAHNLNMRA IAEGVETEDE AVLLYSLDVD EIQGYWMARP QTAEAVERLF DQPTLLDPAT
     FMQRDALPVV LLVEDEEVTL RIMENLLVSF GVKVVSASSA EQAVELFHKY PYAVAIVDHW
     LPGENGIQLL GQIRRLMPQT VRVLVTASND PHVLRDAINV GGAAHFLSKP VDPEALRNVI
     LDACWSQMVR HKSFRPSGY
//
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