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Database: UniProt
Entry: K6T2T7_9CLOT
LinkDB: K6T2T7_9CLOT
Original site: K6T2T7_9CLOT 
ID   K6T2T7_9CLOT            Unreviewed;       959 AA.
AC   K6T2T7;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=PAS domain S-box/diguanylate cyclase (GGDEF) domain-containing protein {ECO:0000313|EMBL:EKQ53618.1};
GN   ORFNames=A370_03663 {ECO:0000313|EMBL:EKQ53618.1};
OS   Clostridium sp. Maddingley MBC34-26.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ53618.1, ECO:0000313|Proteomes:UP000001325};
RN   [1] {ECO:0000313|EMBL:EKQ53618.1, ECO:0000313|Proteomes:UP000001325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX   PubMed=23405323;
RA   Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA   Midgley D.J., Hendry P.;
RT   "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT   Seam Gas Formation Water.";
RL   Genome Announc. 1:E00081-12(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EKQ53618.1}.
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DR   EMBL; ALXI01000112; EKQ53618.1; -; Genomic_DNA.
DR   AlphaFoldDB; K6T2T7; -.
DR   STRING; 1196322.A370_03663; -.
DR   PATRIC; fig|1196322.3.peg.3577; -.
DR   eggNOG; COG5001; Bacteria.
DR   Proteomes; UP000001325; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; 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   CDD; cd00130; PAS; 1.
DR   CDD; cd12914; PDC1_DGC_like; 1.
DR   CDD; cd12912; PDC2_MCP_like; 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   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR033479; dCache_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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   NCBIfam; TIGR00254; GGDEF; 1.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR   PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00563; EAL; 1.
DR   Pfam; PF00990; GGDEF; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   SMART; SM00052; EAL; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF141868; EAL domain-like; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 2.
DR   PROSITE; PS50883; EAL; 1.
DR   PROSITE; PS50887; GGDEF; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001325};
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..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          316..368
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          401..472
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          475..527
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          559..692
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   DOMAIN          701..954
FT                   /note="EAL"
FT                   /evidence="ECO:0000259|PROSITE:PS50883"
FT   COILED          360..394
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   959 AA;  108921 MW;  2448DD448C6CF2F1 CRC64;
     MHIKKKLPIT MIILISIPLL ILSYAIYNYT YMSVTNDSEN HIKQVTSIEG NALSTFVNYQ
     IKEVELSARI ESVVELLKEA KQSEDLKQLI YKTEALNVDK LLTLRVKELN DVQHSFVCDL
     KGNIIADSNS TGLMLNITDR EYFQQAINGE IAISDEIKSK ISNEDIIVVA SPVIDEQGNV
     IGLYCNAIQI SAFNKYIENI TIGNTGYAYL VDDDGIMIAH PQKDKLGKPV ENSVLTKVVD
     EKSYLNQTDT GFDTYVYNGT KKYFGYTVIP KINWILAVTQ NVDEVNAPAR LELYFIMGIT
     LIMLVITSII SLLFSKSITN PISGLIAIMN KAENGDLSVS CDYDSNNELG KLSNNFNSMI
     KKLSGSYEEL SAVYEELSAT EEELRCQYEE LVENEKALAI SEDRFKQALD GINDVIWEWD
     IKANTFFASD KWEELTGYSN KNIDIKNFLK IILPNEELER IVKNYKTLTM SAEYFREEFE
     ITTKSGDKKW ILNRARITMD SEGNPIKITG TISDITSIRQ ANDKIMELAY CDSLTGIPNR
     TTLMSKLDEV INECVENNKL GAALFIDLDD FKRINDSLGH DIGDKLLKRI CTKAKSILNQ
     NEILYRFGGD EFLILMCNVK AREQVINLSN KLLNIFKNYF IIDNKQVYIT CSIGICIFPT
     DGKDKNSILK NADTAMYKAK EKGKNTFEFY NEEMSKKILK DMIIEKALRN GIENNYFYLQ
     YQPQVNIEGK IIGVESLVRL KNEELGFVSP GEFIPIAEKT GLIITIGDWI METAIIKKLE
     WLNNGYGDIR VSINVSSLQI HRPDFVEKVK KLVEKYKINP NFIELEITES VLMEQLDKNV
     VILQELRDIG IRIALDDFGT GYSSLNYLRT IPLNTLKIDK SFIDDICIND KQGAIVDSII
     EMAHKLGMEV VAEGIETIDQ LKVMKEKNCD IIQGYVYSRP LLSTDLENLL KKGFDNLIK
//
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