ID T0GZG7_9LEPT Unreviewed; 750 AA.
AC T0GZG7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Adenylate/guanylate cyclase catalytic domain protein {ECO:0000313|EMBL:EQA72711.1};
GN ORFNames=LEP1GSC059_2463 {ECO:0000313|EMBL:EQA72711.1};
OS Leptospira noguchii serovar Panama str. CZ214.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1001595 {ECO:0000313|EMBL:EQA72711.1, ECO:0000313|Proteomes:UP000015442};
RN [1] {ECO:0000313|EMBL:EQA72711.1, ECO:0000313|Proteomes:UP000015442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CZ214 {ECO:0000313|EMBL:EQA72711.1,
RC ECO:0000313|Proteomes:UP000015442};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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:EQA72711.1}.
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DR EMBL; AKWY02000014; EQA72711.1; -; Genomic_DNA.
DR RefSeq; WP_002177815.1; NZ_AKWY02000014.1.
DR AlphaFoldDB; T0GZG7; -.
DR GeneID; 23201045; -.
DR Proteomes; UP000015442; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00672; HAMP; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 171..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 455..507
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 539..671
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 750 AA; 85349 MW; EF8931B6FEA84D6C CRC64;
MTEQKTFLFC SRLKEGGMLD RWKNKNDKSV RWEELPNLHS DLQDLDLIIR SLISEKLSLG
IREIVFCLSA EQALSLKKSR NFLKLIKDLK RAGFTISSAD RDKILSANVE SSSKFFRYLE
NRSRNTNCLV WTEISELSQI ESKYYDFLNH FRQINGDQSF RPSRFTIRVK LLSIVSAIIT
LSMGLMITMA TYFFRKYSEI LIQEYNLSLA RMTGLQLSGQ LKETTRKIQD FRSEDSEKFF
KTNSNAVAYV RFKSKAVNSV WEIDSLFWNS KFLKSNSVVL DSTHLKKALE KSFSRLSNTL
EILNVSSEFG FPAVAVLLPI DDKICGLVFS ASEFLGSFLS VRQTDFFQMI VVDSSGNLIA
HSNDKEAVSG KDYKKHPLVE NMLRSPSDNG SQRFDFEGRE VLGSYQQLEV GGLGIISTLD
ADIAFEAVYQ IRRQNLWIMI SVLSVAFFVV FVFSRTLTIP IIQLLSATKK VEQGDYVVDI
RATTHDEVGV LTNSFLRMAR GLEEREKIKN TFGKFVNKEI AERALSSDLK LGGENREVTV
FFSDLRNFTG MSEKMKPEEV VEFLNQYFTE MVECIYLTQG IVDKFIGDAV MAHWGALVHD
GNEAKNSINA ALLMRRALIE FNLKGKEIGR PFTRFGCGIN SGPVIVGQIG SEKKLEFTVI
GDAVNLASRI EYLNKEFGTD ILISESTYQQ TKDHFNFVEL PPVWIRGKEK PQVIYAVLGW
KEDQDCPKSL EELRTLCDIP DPENPSRSLA
//