ID L7VFI9_MYCL1 Unreviewed; 510 AA.
AC L7VFI9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Transmembrane protein {ECO:0000313|EMBL:AGC64179.1};
GN OrderedLocusNames=MULP_04666 {ECO:0000313|EMBL:AGC64179.1};
OS Mycobacterium liflandii (strain 128FXT).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=459424 {ECO:0000313|EMBL:AGC64179.1, ECO:0000313|Proteomes:UP000011157};
RN [1] {ECO:0000313|EMBL:AGC64179.1, ECO:0000313|Proteomes:UP000011157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=128FXT {ECO:0000313|EMBL:AGC64179.1,
RC ECO:0000313|Proteomes:UP000011157};
RX PubMed=23204453; DOI=10.1128/JB.02132-12;
RA Tobias N.J., Doig K.D., Medema M.H., Chen H., Haring V., Moore R.,
RA Seemann T., Stinear T.P.;
RT "Complete Genome Sequence of the Frog Pathogen Mycobacterium ulcerans
RT Ecovar Liflandii.";
RL J. Bacteriol. 195:556-564(2013).
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; CP003899; AGC64179.1; -; Genomic_DNA.
DR RefSeq; WP_015356956.1; NC_020133.1.
DR AlphaFoldDB; L7VFI9; -.
DR KEGG; mli:MULP_04666; -.
DR PATRIC; fig|459424.11.peg.4806; -.
DR HOGENOM; CLU_562374_0_0_11; -.
DR Proteomes; UP000011157; 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, ECO:0000313|EMBL:AGC64179.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..293
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 326..451
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 510 AA; 54007 MW; BB4A88DD3C24F97E CRC64;
MERVWQWAWD RCGARYSWAI CVVTFAVVLP VYLLLSFWVV AFENSGHYIE AAVVTVAVVS
LGLWVIFLPS VVRRRLPEKW AADHDVDRLS ALEATYVYGR GAVVRGLGSN VVLGAFNLVA
VGAVAGASGS RLVQYGIVGA ATGIGIQLIA IHSFVEAALR PVRVAIIGDT AIGDSLPRSR
PTFAAWSNLS VFGVAFNFAI VGAMLAGLIS QAHTVPLVSL VIGAGMAVVF GVPVIVAPSF
SPSMQPIRDL AAGTERVAAG DYSRRLPVVQ DDDLGALAAS FNHMQAGLVE RQRLQAAFGT
YVDPGLAARL LEQGDDVFTG ERRQVTVMFV DVRDFTPFAE AHTAEDTVSR LNELFEIVVP
TVVDAGGHVN KFLGDGALAV FGAPNDLADH ADAAVAAAVL IHRRVVERFG EEFRIGIGIN
TGVVIAGTIG GGGKLEFTLI GDTVNVAARV EQLTKATGDA ILLTQQCVDA QGSRPAGLID
RGLHVLKGKS AAIQVFGLHQ ESDMRADLTH
//
