ID A0A0A2WLK1_BEABA Unreviewed; 1107 AA.
AC A0A0A2WLK1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Probable transcriptional regulator ycf27 {ECO:0000256|ARBA:ARBA00015955};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=OmpR-like protein {ECO:0000256|ARBA:ARBA00032623};
GN ORFNames=BBAD15_g67 {ECO:0000313|EMBL:KGQ13989.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ13989.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ13989.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ13989.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable promoter-specific protein mediating the interaction
CC between DNA and RNA polymerase. {ECO:0000256|ARBA:ARBA00003612}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SIMILARITY: Belongs to the peptidase U32 family.
CC {ECO:0000256|ARBA:ARBA00038374}.
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:KGQ13989.1}.
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DR EMBL; ANFO01000008; KGQ13989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2WLK1; -.
DR STRING; 1245745.A0A0A2WLK1; -.
DR HOGENOM; CLU_282272_0_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19938; REC_OmpR_BaeR-like; 1.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.690; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR001539; Peptidase_U32.
DR InterPro; IPR032525; Peptidase_U32_C.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR30217; PEPTIDASE U32 FAMILY; 1.
DR PANTHER; PTHR30217:SF6; TRNA HYDROXYLATION PROTEIN P; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01136; Peptidase_U32; 1.
DR Pfam; PF16325; Peptidase_U32_C; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS01276; PEPTIDASE_U32; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU01091}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KGQ13989.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 139..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 158..210
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 218..431
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 435..548
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 554..658
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DNA_BIND 554..658
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT MOD_RES 484
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1107 AA; 124629 MW; 646850DB81C20630 CRC64;
MHWGVRLSFE RGFIDYIKRG NAQRIEMLSD ALGEQYALHG NWRFLLHNDR FVFQILRSFE
REGDEGRGLP PHGWRTKFWV VDQNYQVLVG PREKLPRDGM RKSINVNGQD VGWVVASPIE
RLTRNTDINF DRQQRRTSWI IVALSSLLAA AATFLLARGL LAPVKRLVEG THKLAAGDFS
TRVAVGSQDE LGRLAQDFNQ LASTLEKNHK MRRAYMADIS HELRTPLAVL RGELEAIQDG
VRKFTPESVT SLQMEVATLT KLVDDLHQLS MSDEGALAYQ KKSLDIIALL EVVAGAFRSR
FDSRGLTIRL ALPDTAIIFG DGDRLMQLFN NLLENSLRYT DSGGQLVISA KIINQQFVMS
FDDSEPGVSD EQLSQLFDRF YRAEGSRNRA SGGSGLGLSI CQNIVTAHGG TLTASHSRFG
GDTMTELPID DSTPRILIVE DEPKLGQLLI DYLRAASYAP TLLTHGDQVL PYVRHTPPDL
ILLDLMLPGT DGLTLCKEIR RFSEVPIVMV TAKIEEIDRL LGLEIGADDY ICKPYSPREV
VARVKTILRR CKRQMAISAG SEESPLVIDE GRFQAIWRGK LLDLTPAEFR LLKTLSHEPG
KVFSREMLLN HLYDDYRVVT DRTIDSHIKN LRRKLEALDT DQSFIRAVYG TETFMFKPEL
LSPAGTLKNM RYAFAYGADA VYAGQPRYSL RVRNNEFNHE NLQLGINEAH ALGKKFYVVV
NIAPHNAKLK TFIRDLKPVI DMGPDALIMS DPGLIMMVRE AFPAMDIHLS VQANAVNWAT
VKFWKQMGLT RVILSRELSL EEIAEIREQV PEMELEIFVH GALCMAYSGR CLLSGYINKR
DPNQGTCTNA CRWEYKVQEG KEDDIGNIVH VHEPIPVQNV EPTLGVGAPT DKVFMVEEAK
RPGEYMTAFE DEHGTYIMNS KDLRAIEHVE RLTKMGVHSL KIEGRTKSYY YCARTAQVYR
RAIDDAAAGK PFDPTLLQTL EGLAHRGYTE GFLRRHTHDS HQNYEYGHSI SESQQFVGEF
TGERRGDLAA VAVKNKFLLG DSLEMMTPQG NITFTLETLE NGKAQPIDVA PGDGHTVWMP
VPQEIALDYA LLMRNLSGQT TRKPHAN
//
