ID I3TWK2_TISMK Unreviewed; 590 AA.
AC I3TWK2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=diguanylate cyclase {ECO:0000256|ARBA:ARBA00012528};
DE EC=2.7.7.65 {ECO:0000256|ARBA:ARBA00012528};
GN Name=ydaM {ECO:0000313|EMBL:AFK57140.1};
GN OrderedLocusNames=TMO_c0530 {ECO:0000313|EMBL:AFK57140.1};
OS Tistrella mobilis (strain KA081020-065).
OG Plasmid pTM3 {ECO:0000313|EMBL:AFK57140.1,
OG ECO:0000313|Proteomes:UP000005258}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK57140.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK57140.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC PLASMID=Plasmid pTM3 {ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003239; AFK57140.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TWK2; -.
DR KEGG; tmo:TMO_c0530; -.
DR HOGENOM; CLU_000445_134_0_5; -.
DR Proteomes; UP000005258; Plasmid pTM3.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR029151; Sensor-like_sf.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR PANTHER; PTHR45138:SF9; DIGUANYLATE CYCLASE DGCM-RELATED; 1.
DR PANTHER; PTHR45138; REGULATORY COMPONENTS OF SENSORY TRANSDUCTION SYSTEM; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00990; GGDEF; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Plasmid {ECO:0000313|EMBL:AFK57140.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 330..383
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 458..590
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT COILED 403..430
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 590 AA; 64382 MW; DD01717C0A924F5F CRC64;
MATATGPDRG IRRPRRLGRP GLRTLLTVTM AGLALTTVVL LALVVAEVAG RRQAAEIGDS
LDELAFQMSD KLDRAMFERW RDIRIIAARP VLRGDDTAAK RVALEILQQT YPDYAWIGFT
DVQGRVLAST GRLLEGEDVS ARPWFVGALK GPFAGDVHKA LLLERLLTNP DPGTPLRFVD
VSMPVMAEGG LIGVVGAHLS WSWADDIRRS LIAPGESRSG TDILVVDKDG AVLLGPRALE
GQKLDLPGLT AGSRDPGPWV ETWPDGDRAY LTALHRSQGF RDYPGLGWTV VVRQPVDQAL
APVRDLRRLI LWGAVAIAAT ACGFALWLAA RIASPLDRLS RAARRVGETS SPDEVPLDGG
YREVRDLAWS LQRMIAALTQ KQEELVRANL GLEARVAERT AELTAEIAER RKVEQDREDL
IQRLKRMAET DFLTGVMNRR SFFDIAGREL AAARRYVRAL AVIVLDIDHF KRINDRYGHG
TGDEILKGVA KRLADEMRAG GILARFGGEE FVILLQEADQ DAALATAERL RTALADRSFG
LIDGSCLTVT ASLGLATADS ETGSIDDLIT RADAALYRAK DAGRNRVEAG
//