ID U5W858_9ACTN Unreviewed; 794 AA.
AC U5W858;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Signaling protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AFR_35365 {ECO:0000313|EMBL:AGZ45329.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ45329.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ45329.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ45329.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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DR EMBL; CP006272; AGZ45329.1; -; Genomic_DNA.
DR RefSeq; WP_023561665.1; NC_022657.1.
DR AlphaFoldDB; U5W858; -.
DR STRING; 1246995.AFR_35365; -.
DR KEGG; afs:AFR_35365; -.
DR PATRIC; fig|1246995.3.peg.7156; -.
DR eggNOG; COG5001; Bacteria.
DR HOGENOM; CLU_000445_91_5_11; -.
DR OrthoDB; 9763119at2; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:UniProt.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR PANTHER; PTHR33121:SF85; CYCLIC DI-GMP PHOSPHODIESTERASE PDEK-RELATED; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 306..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 397..530
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 539..787
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 794 AA; 85389 MW; DE960E7CAB6E1363 CRC64;
MRSTSLGSNR RRWSGVALVV VVALLGTAVA WVATGNARRA EQRYAAQLMD RYTSDLTRAI
TTEIQRYGDT LDDVATALGA QTDLTADDFG WITNKISNRR LPGATSLGFV VSTPDSGVGA
LQSYWRERGA SNLMLSPVDT AGEHAFAVFT RSFDGVPVVA GMDLSAAPEA SDALQDAQFL
GGFAVSRAYV LLKDRALPVT QQQLSFLFAV PVYRIGGAFR GWLTMGVHGR DLLTETLRTQ
SHGAVTAGLE DPTDRVERTI ASASGGKARN YPAALDRTAS VSAGLRTWRL EVHPTDQLLE
ETDRGIVGTT FAVAMTITLL LTLLVALLAG ARNRAMSKVD AATAALRSDI ERRQQVETRL
RERELELEQM ALHDPLTGLA NRAGLDARLA EVVGTRSDVA LLLIDLDDFK LVNDAYGHAA
GDAMLTEFAQ VLLAGVRTGD VAARIGGDEF VVLITDVPDD ARAVAAAQRV LAAAASAPVR
LGDDTLPVRA SIGVATSRAG DSPKELLRRA DIAMYQAKHL GTHGVQLHDP SMTDRRKADS
LLAEDLAGAL DRDELHVLYQ PLVDLTDSRP IGVEALIRWR HPRLGLVSPA DFIPIAERTG
TITAIGLWVL ETACREITRW DGLYVSVNLS PRQLQEPTLV QDVLGVLART GLAPDRLVLE
ITESALVDES AGIAMLQEFR EHGIRVAIDD FGTGYSSLHY LTRLPVDILK IDRSFVAELN
GTPEGSGITE AILRLSQVLH LTAIAEGIET AEQAAELQLL GCGVGQGYLF ARPLPPTELQ
DLLLSPSPRP SSLS
//