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Database: UniProt
Entry: C6HZ78_9BACT
LinkDB: C6HZ78_9BACT
Original site: C6HZ78_9BACT 
ID   C6HZ78_9BACT            Unreviewed;       500 AA.
AC   C6HZ78;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Diguanylate cyclase with PAS/PAC sensor {ECO:0000313|EMBL:EES52089.1};
GN   ORFNames=UBAL3_94530055 {ECO:0000313|EMBL:EES52089.1};
OS   Leptospirillum ferrodiazotrophum.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=412449 {ECO:0000313|EMBL:EES52089.1, ECO:0000313|Proteomes:UP000009374};
RN   [1] {ECO:0000313|EMBL:EES52089.1, ECO:0000313|Proteomes:UP000009374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19429552; DOI=10.1128/AEM.02943-08;
RA   Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M.,
RA   Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J.,
RA   Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., Banfield J.F.;
RT   "Community genomic and proteomic analyses of chemoautotrophic iron-
RT   oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum
RT   ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms.";
RL   Appl. Environ. Microbiol. 75:4599-4615(2009).
CC   -!- SIMILARITY: Belongs to the hemerythrin family.
CC       {ECO:0000256|ARBA:ARBA00010587}.
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DR   EMBL; GG693880; EES52089.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HZ78; -.
DR   Proteomes; UP000009374; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01949; GGDEF; 1.
DR   CDD; cd12107; Hemerythrin; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 1.20.120.50; Hemerythrin-like; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR000160; GGDEF_dom.
DR   InterPro; IPR012312; Hemerythrin-like.
DR   InterPro; IPR035938; Hemerythrin-like_sf.
DR   InterPro; IPR012827; Hemerythrin_metal-bd.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   NCBIfam; TIGR00254; GGDEF; 1.
DR   NCBIfam; TIGR02481; hemeryth_dom; 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; PF00990; GGDEF; 1.
DR   Pfam; PF01814; Hemerythrin; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47188; Hemerythrin-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50887; GGDEF; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009374}.
FT   DOMAIN          190..238
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          346..494
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
SQ   SEQUENCE   500 AA;  55209 MW;  3C43C13494F0A21D CRC64;
     MPDSPAQEDE NFATGFEEID RQHRGLVELV NRLPALSAGV PGAPELAVIL SELRSYVVVH
     FSTEEILWER IPHEGPLAPL LSAHEEAHRD FSRKVAELGR SPEPEEVGKI VHFLTHWLAR
     HILESDRRMA FVLKGVEKGL SPGEALVLAE QNLDLTAAFT RTVLSMYDQV VDQALRLIEE
     ISRRQSVEES LRLLGQIFES VRDGILLLDP DGTIVDANPS FRRQIPDLPD DLVGRSIFAS
     PPLFDHETLS RAFQEVRKTG HFSGTIRTFK KEGESDNLWI SLSSVVGKGG ETTHMTAIFS
     PVSELLEENE VLSEAANSDP LTDIPNRRLF NDRFARALRE AASGKHRGAL ILIDLDRFKA
     LNDLRGHPAG DEVLRESARR LRESVRQSDL VARLGGDEFA VLLGGLHPER KAAALEARSA
     AEKIRLSLAR PFEVMTRDET GKKSSFRHFC PPSLGVAVFG GEGRGKEPEV FGAADRALYR
     GKDRGGNTVV VAGEEISASS
//
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