ID C3G4S5_BACTU Unreviewed; 868 AA.
AC C3G4S5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding {ECO:0000313|EMBL:EEM71324.1};
GN ORFNames=bthur0009_28210 {ECO:0000313|EMBL:EEM71324.1};
OS Bacillus thuringiensis serovar andalousiensis BGSC 4AW1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM71324.1};
RN [1] {ECO:0000313|EMBL:EEM71324.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM71324.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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:EEM71324.1}.
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DR EMBL; ACNG01000072; EEM71324.1; -; Genomic_DNA.
DR RefSeq; WP_000094197.1; NZ_CM000754.1.
DR AlphaFoldDB; C3G4S5; -.
DR HOGENOM; CLU_005950_0_0_9; -.
DR Proteomes; UP000001380; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EEM71324.1};
KW Pyruvate {ECO:0000313|EMBL:EEM71324.1};
KW Transferase {ECO:0000313|EMBL:EEM71324.1}.
FT DOMAIN 17..316
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 792..863
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT REGION 412..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 48..75
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 868 AA; 97569 MW; C44601A33BE66949 CRC64;
MSSFVLDFQE IEKTQLSLVG GKGLNLGALS NMQEIQVPEG FCVTTVGYEK AVEQNEELQT
LLQQLTKLKR EERVRIGEIS KKIREVIMAV QIPSDVVEAV AHYLSRFGNE HAYAVRSSAT
AEDLPYASFA GQQDTYLNII GENAILQHVK KCWASLFTER AVMYRMQNGF EHNQVSICVV
VQKMVFPQAS GILFTADPIT SNRKVLSIDA SFGLGEALVS GLVSADNYKV KEGEIIDKMI
ATKKLAIYAL KEGGTETKQN DSVQQKIQTL SDQQILQLVQ IGRQIEAYFG CPQDIEWCLV
DHTFYIVQSR PITTLYPIPE ENDEGNHVYI SVGHQQMMTD AMKPLGLSFF LLTTNAPMRK
AGGRLFVDAT QQLALPASRD YLINTLGKSD PLVRDALTTI IERDNFITLL PDEEKEKSAS
KSKPPVSSQP EIENDPAIVT ELIRNSEASL EELKQNMQLK SGVDVFDFIL EDIQQLKKVL
FNPQSIAVIM AGMNASTWIN EKMEQWLGEK NAADTLSQSV QNNITSEMGL ALMDVADAIR
PYPEVITYLQ HVEDDSFLDE LVQYKGGEKA RDAIVAFLNK YGMRCSGEID ITKTRWSEKP
TTIIPMILNN IRDFEAGASK QKFEKGLQEA LNKEEELLDR LQHLPKGKQK VEETKRMIRN
IRNFIGYREY PKYGMINRYF IYKQALLKEA EQLVQSGVIR EVDDIYYLTF EELHEVVRTN
KLDYELIQKQ KNDYKLYEKL TPPRVMTSDG EIITGKYKRE NLPADAIVGL PVSSGVVEGR
ARVILNMEDA NLEEGDILVT AFTDPGWTPL FVSIKGLVTE VGGLMTHGAV IAREYGLPAV
VGVENATKLI KDGQRIRVHG TEGYIEVL
//
