ID A0A126T2G5_9GAMM Unreviewed; 1099 AA.
AC A0A126T2G5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Diguanylate cyclase {ECO:0000313|EMBL:AMK76265.1};
GN ORFNames=JT25_007125 {ECO:0000313|EMBL:AMK76265.1};
OS Methylomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK76265.1, ECO:0000313|Proteomes:UP000030512};
RN [1] {ECO:0000313|EMBL:AMK76265.1, ECO:0000313|Proteomes:UP000030512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK76265.1,
RC ECO:0000313|Proteomes:UP000030512};
RX PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA Kits K.D., Klotz M.G., Stein L.Y.;
RT "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT FJG1.";
RL Environ. Microbiol. 17:3219-3232(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP014476; AMK76265.1; -; Genomic_DNA.
DR RefSeq; WP_062328115.1; NZ_CP014476.1.
DR AlphaFoldDB; A0A126T2G5; -.
DR STRING; 1538553.JT25_007125; -.
DR KEGG; mdn:JT25_007125; -.
DR OrthoDB; 8553030at2; -.
DR Proteomes; UP000030512; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:UniProt.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR007895; MASE1.
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 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; PF03924; CHASE; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 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; PS50839; CHASE; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030512};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..466
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 538..586
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 611..665
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 697..835
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 844..1097
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 1099 AA; 123421 MW; 818DEAD8DBAAF61D CRC64;
MSASFRLFLI NGALALAYFA GGYLGHQLAM PPSHASPIWP SAGIALAALL GYGPRILPGL
LIGTLCTQIY AFWDLATAED WFTPIWVGSA ASVGAIAQPL LGAALINRWI GKHNPLMEDR
HIVWFFLLAI ASCLISASVG TSFLYIFDTI DAGEFGLNWC TWWIGDAIGT VIFAPLLLLF
IGTPRHIWRQ RQKFVAYPLS ISLLLVIVAF VYSRSMENQR IDELLENQVN LTHTNLQEHF
GDDILNNQLL KALFDSSESV NPNEFRLFAH TIFTKHPELE ALEWIPRINA DERAAFERQT
ETSIREQAPN QQLIPAGKRN VYLPIAYSFG NQQNIGFDVA SNQQLLAAIN KAIATGETVV
TAGIVCSDNQ PGFAIYSPVY LKGKLLNTSA QRQQFFVGLV ANVFKLSSEV QELSARLQSI
QLSVAIYDQD QLLYSSAREG PELKTHYSPP IRRQALAVAD RSWTLEYQPL PEFYTQQHSW
TVWWLLSGSF LLCGLTGFGL MLMSGRTARI EDLVALKTRD LLRSNQALNT EIERRKQQEN
ELRIAATTFQ SHEAIIVTDA SGAILRVNNA FNKITGYSAE EVIGRQPDFL SSAHQAPGFI
QTLIQALARD NQWQGEILNR RKNGDVFPEW LTVTGVRDEQ DRLLNYVAIF SDISEQKAAE
REIHELAFYD PLTGLPNRRL LLDRLKQEIA AAKRQSYYGS LFFLDLDHFK TLNDSRGHQV
GDELLIQVAQ RLKSIIRDED TACRLGGDEF IVMVPGRYSQ LSQATSHAAM LAEKILHTIN
LPFTVQGSEH HFSTSIGVTL FPEVAEQPEA VIQQADTAMY RAKESGRNGI SFYRPSMQET
ADRRLTLEKE IRQALKQRQF LLHYQAQVDH LGKVVSAEAL IRWQHPEKGM VSPAEFIPIA
EDTQLILPIG EWVMREACRQ IKVWDAQNLP IHHVAVNVSS RQFRQADFVD QVKRILVDAE
LPAERLVIEL TEGCVISDID DTVEKMRDLQ TLGVKTSIDD FGIGYSSLSY LKKLPISQLK
IDQSFVRDIA SDPNDAVIVE TIINMAKNLG LHVIAEGVET QEQLIFLRNK GCLSYQGYYT
GRPVSAARFE LEDRLLPTA
//
