ID G7MBZ4_9CLOT Unreviewed; 934 AA.
AC G7MBZ4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=PTS system transcriptional activator {ECO:0000313|EMBL:EHI97522.1};
GN ORFNames=CDLVIII_0797 {ECO:0000313|EMBL:EHI97522.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI97522.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHI97522.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI97522.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001240; EHI97522.1; -; Genomic_DNA.
DR RefSeq; WP_009168204.1; NZ_CM001240.1.
DR AlphaFoldDB; G7MBZ4; -.
DR STRING; 641107.CDLVIII_0797; -.
DR eggNOG; COG1221; Bacteria.
DR eggNOG; COG3933; Bacteria.
DR HOGENOM; CLU_014204_1_1_9; -.
DR Proteomes; UP000005106; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd00006; PTS_IIA_man; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR Gene3D; 1.10.1790.10; PRD domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011608; PRD.
DR InterPro; IPR036634; PRD_sf.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR033887; PTS_IIA_man.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR PANTHER; PTHR32071:SF90; TRANSCRIPTIONAL REGULATORY PROTEIN LEVR; 1.
DR Pfam; PF03610; EIIA-man; 1.
DR Pfam; PF00874; PRD; 2.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR SUPFAM; SSF63520; PTS-regulatory domain, PRD; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51372; PRD_2; 2.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 111..345
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 469..574
FT /note="PRD"
FT /evidence="ECO:0000259|PROSITE:PS51372"
FT DOMAIN 575..716
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 837..934
FT /note="PRD"
FT /evidence="ECO:0000259|PROSITE:PS51372"
SQ SEQUENCE 934 AA; 105577 MW; 29B1C6CE215D9BBB CRC64;
MKQIEKIYNY ILLKSKEFTK EKLLEVKGFS AQQIGEHFGV LRSNVSRELN NLCREKKIIK
IKNRPVLYFE KEQFIKLLNI KGVFDYEEGI DIKDFIDISD EKKDRSSFNS LIGFNRSLKN
QIEQAKAALL YPPNGLHTLI IGGTGVGKSL FANMMYKYYK SIKELPEDPP FIIFNCADYC
NNPQLLLSHI FGHVKGAFTG AEKEKEGIVE KADGGILFLD EIHRLPPEGQ EMVFYFMDTG
TYNKLGETDR RRRANVLLIG ATTEDPNSTL LNTFIRRIPI TITIPAFDER SIDEKLELVQ
YLFSKEAQRV NKAIRISSEA IKALIGSTTY GNVGQLKSNI QLVCAKGFFN SVNTDKNIEI
NLTLLPPNIK SGILAFGNQT GDNTTMWNMM PNSITIQPDG NKTFLETDDY ETPFNIYSII
ENKTSLLKEE GLDDNEINSF ITTDINIHLK QFYDRFKNDI NRREGLLKIV DKDIIDFAEE
IKKIAETRLN RKLNERFIYA TSLHFSALFN RIKKNTVSLE SNITLSISAE SNEYKVAKEI
HKLIQKNFNL IIPDVEIEYL ALLLSSIQES SRQERVGIVV ASHGVNIATS MVSLAKKLFE
ADNILAVDMP LERSPADILD TVIEKVKLVD EGKGVLLLVD MGSLNSFGEV IKEKTGIEIK
SIDMVSTPLV LEAVRKCSVC DVDLNSVYSY LLTDFRGYSN NISEYITKNK KQKEKVIVTV
CSTGKGAALK LKVLVENVIR NISTEKINVV SLGVKNLKDS ITHISKESNI LAVIGISNPK
LGIPFISIEQ LIDGSGENTL VSILEGKNIK PVESKGNKQV IFKDLCIQNL SEIITFLNPK
KIYSLLDEFL HLIEKSLNIS FQNSAKLRIM FHVACALERM IRNNGLVYDE ENINFDEKTI
QVLKEASLIF KDALSIKLTD DEIYFIADII KMTD
//