ID G2FDI9_9GAMM Unreviewed; 663 AA.
AC G2FDI9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative signaling protein {ECO:0000313|EMBL:EGW55044.1};
GN ORFNames=TevJSym_af00080 {ECO:0000313|EMBL:EGW55044.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW55044.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW55044.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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:EGW55044.1}.
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DR EMBL; AFZB01000006; EGW55044.1; -; Genomic_DNA.
DR AlphaFoldDB; G2FDI9; -.
DR PATRIC; fig|1049564.3.peg.972; -.
DR eggNOG; COG5001; Bacteria.
DR Proteomes; UP000005167; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR PANTHER; PTHR44757:SF2; BIOFILM ARCHITECTURE MAINTENANCE PROTEIN MBAA; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF00672; HAMP; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 176..228
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 267..400
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 409..662
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 663 AA; 74222 MW; 6407B020B62DA136 CRC64;
MGNPRNNFTF SQLPIWRQIL LLLGGSILLV GYAVGIVFEQ LETDYLRQNL EEQNHRILSV
LSATSIDAVI SEDQARLETI ITQLATLDPN ILSLTMENER RETLAHWQRI SDTGAMTHLA
FAEDILFDGE HFGRIFIDWN IQPLQQQIDL HVLSMRLFST AVLIALTGLI LFWIYLLISK
PINTLNKRLH MIAQGDLTSE VHISSGKELI RLADSVNTLS RILRINESRK KEIRQLAFFD
KTTGLASRAH FLQRFSDTLK AATRRDEQLA LIFLDLDGFK DINDSMGHET GDQLLAIIGQ
RLEKPLRDVD FAARFGGDEF CIIVDNITDE FDAAEVADRC LKEIHQPVEL GTQTVRPMAS
LGIALFPKDG NDMQQLLKAA DSAMYAAKEA GKHRYAFYIP ELTTQASQRL ALEQQLRVAV
DNNDFTLHYQ PQISLSSGKV TGVEALIRWH HTELGDIPPS EFINLAERIG LIQEIGEWVL
ETACRQAASW HHNALDQLQV AVNISAIHFT DLDFVNTVTR VLDTTGIDPK RLEIEVTESV
IQLGDNYSTT CQQLDALGIK VAVDDFGTGY SSLAVLKQLP IDTLKVDRLF IKDLQHEAKS
TVLVGTIIGM AQALGYKVVA EGAETLEQIQ ILRGLGCHQV QGYYFSPPVP ADQIPSLVSK
VHF
//