ID L0J2K9_9MYCO Unreviewed; 481 AA.
AC L0J2K9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Family 3 adenylate cyclase {ECO:0000313|EMBL:AGB24832.1};
DE Flags: Precursor;
GN ORFNames=Mycsm_04598 {ECO:0000313|EMBL:AGB24832.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB24832.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; CP003078; AGB24832.1; -; Genomic_DNA.
DR RefSeq; WP_015308408.1; NC_019966.1.
DR AlphaFoldDB; L0J2K9; -.
DR STRING; 212767.Mycsm_04598; -.
DR KEGG; msa:Mycsm_04598; -.
DR PATRIC; fig|710686.3.peg.4630; -.
DR HOGENOM; CLU_025433_2_0_11; -.
DR OrthoDB; 368920at2; -.
DR Proteomes; UP000010844; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 6.10.340.10; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF17; BLL5647 PROTEIN; 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 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..278
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 310..432
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 481 AA; 51563 MW; FC0FF2BC735CABDD CRC64;
MRPPSLLVRY AAGLAFAYLL SAAEVVAIVI SVSRETVLEA QSVLNVTNLV ATAAIIVVGT
LSVGLSGAAL VARALGRAAN PQKTANITRR QSAILLAPWA LAAAVMVPLN FSAGLRVLIL
IVSAIMFGST ATVCTGFLFT QRALRALMVA ATWDLEHAER APGVRARLIL MWTMCSALPG
AGIVVLVMLR ANGWIIQRDA PIEVPVLVLA SVAVVLGMRA MILVASSISD PIHDVVDAMA
EVERGHLGNK IEVYERSELG QLQSGFNRMV AGLQERDRLR DLFGRHVGEE VVRRAIEEHE
SVSEDERDVA ILFIDLVGST QFAATHEPHQ VAAVLNDFFR IVVAEVDKRE GLINKFQGDA
ALAVFGAPLH IDDPATAALA TARALAEQLR LLLVDFGIGV SAGPVFAGNI GAENRYEYTV
VGDAVNEAAR LADRAKEFES RVLCSSAAID RADEAERRCW KLEGSEMLRG RSELTQISAP
V
//