ID A0A5Q0BIX8_9GAMM Unreviewed; 772 AA.
AC A0A5Q0BIX8;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Diguanylate cyclase {ECO:0000313|EMBL:QFY43770.1};
GN ORFNames=F6R98_14995 {ECO:0000313|EMBL:QFY43770.1};
OS Candidatus Methylospira mobilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylospira.
OX NCBI_TaxID=1808979 {ECO:0000313|EMBL:QFY43770.1, ECO:0000313|Proteomes:UP000325755};
RN [1] {ECO:0000313|EMBL:QFY43770.1, ECO:0000313|Proteomes:UP000325755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shm1 {ECO:0000313|EMBL:QFY43770.1,
RC ECO:0000313|Proteomes:UP000325755};
RA Oshkin I.Y., Dedysh S.N., Miroshnikov K., Danilova O.V., Hakobyan A.,
RA Liesack W.;
RT "Ecophysiology of the spiral-shaped methanotroph Methylospira mobilis as
RT revealed by the complete genome sequence.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP044205; QFY43770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q0BIX8; -.
DR KEGG; mmob:F6R98_14995; -.
DR InParanoid; A0A5Q0BIX8; -.
DR OrthoDB; 9813903at2; -.
DR Proteomes; UP000325755; 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; 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; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_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; PTHR46663; DIGUANYLATE CYCLASE DGCT-RELATED; 1.
DR PANTHER; PTHR46663:SF3; DIGUANYLATE CYCLASE DGCT-RELATED; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50839; CHASE; 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:UP000325755};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..475
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 536..582
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 609..661
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 693..772
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 772 AA; 85799 MW; E5DD8763BB90E476 CRC64;
MSRSGITDWI LRFLALTMLI IVTGWLALSL ALPPGYASPI WPPAGIALAA LLMWGRKQWP
AVWIGTYALN LWILGNHPGG NAGNDLFFVA AGEATGSTLQ ALVGAWLTLR WVHPGVPKLS
TPRAILLFAV LTGPLACLIA PSAGIASLMH FNTLPASMAA LIWWNWWVGD TLSAVIIAPI
MFCLFAKPRD FWLPRLLTVA LPLAGSLAVL ISIFIFIFRT GESNIQAQFN NEATRFANAI
TENVDRTIDA SVTVAPPKRS EFAAFTSGIL QRNPEIQMLE WIPRITREQR GRFEQSVRAE
GYKDFSIKDQ APGDALVPAA DRKEYFPVLF MEPMTVNPQA LGFDMASEPI RRQTLETAQA
SGKPVVSQRI DTLPGEPDLH YRVLMVTPVY DDLPHTSQKN LIGFTVASVR LDRLVETALT
EFDWRGLHLT ISDSSAPPET ADLFREDRNW NEAADFHLHN WQKTLTVADR TWRLTISPDA
DFVSRHSAWL PWVTQANGLA LACILTFYLL MITGRTAHIQ AIVTERTASL EAANKQLKLA
ARVFTEAREG IIISDADGMI VDVNPTFSEI TGYSREEAIG QTTHILKSDG QNPEIYAQIW
KTLTQQGHWQ GELWNRKKSG ELYAELLSFS ALRDEKGQIR NFIGLFSDIT PLKQQQQALE
LLAYHDPLTN LPNRTLFEDR FTQAIARCNR DKSLLAICYM DLDGFKQVND QMGHEAGDQL
LIEVSQRLVA SLREGDTAAR LGGDEFALLI NICNDPQSKT HEPAISASAN PD
//
