ID A0A162QTV1_9CLOT Unreviewed; 915 AA.
AC A0A162QTV1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Transcriptional regulatory protein QseF {ECO:0000313|EMBL:KZL88959.1};
GN Name=qseF {ECO:0000313|EMBL:KZL88959.1};
GN ORFNames=CLMAG_56500 {ECO:0000313|EMBL:KZL88959.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL88959.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL88959.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL88959.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZL88959.1}.
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DR EMBL; LWAE01000012; KZL88959.1; -; Genomic_DNA.
DR RefSeq; WP_066630156.1; NZ_LWAE01000012.1.
DR AlphaFoldDB; A0A162QTV1; -.
DR STRING; 1121326.CLMAG_56500; -.
DR PATRIC; fig|1121326.3.peg.5712; -.
DR OrthoDB; 9765164at2; -.
DR Proteomes; UP000076603; Unassembled WGS sequence.
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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd00133; PTS_IIB; 1.
DR Gene3D; 3.40.50.2300; -; 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; 1.
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; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR002078; Sigma_54_int.
DR PANTHER; PTHR32071:SF38; PSP OPERON TRANSCRIPTIONAL ACTIVATOR; 1.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF03610; EIIA-man; 1.
DR Pfam; PF00874; PRD; 1.
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; SSF52794; PTS system IIB component-like; 1.
DR SUPFAM; SSF63520; PTS-regulatory domain, PRD; 1.
DR PROSITE; PS51372; PRD_2; 2.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076603};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 103..337
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 449..559
FT /note="PRD"
FT /evidence="ECO:0000259|PROSITE:PS51372"
FT DOMAIN 560..686
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 816..915
FT /note="PRD"
FT /evidence="ECO:0000259|PROSITE:PS51372"
SQ SEQUENCE 915 AA; 105718 MW; 9254EE5D8C062282 CRC64;
MGIDISRYLK EITKEFNKEN LKQFSANSIA EIVELSRSTV SSYLNKECKR GTIIKIKEYP
VIFLDKETFS NVHFTPMHNE YDTFDELWQE GSKIKKVDTW SKVIGSKGSL KEQIEQIKTA
VLYPENGLPI MLLGSSGSGK TYLAKCIYDY CFGEKLIDPK AKFISLNCAQ YYHNPELLSS
LLFGYTKGAF TGADRDKIGL LESADGGVLF LDEVHRLTEE GQEKLFTFMD SREYSPIGDN
SIKKEAKVRL IFATTESIQS AFLPTFIRRL PVIVNIPSFA ERPQQERIHL IDSFFLKESE
ILQRTIQVTK QVMSFLLFSN YEGNVGKIKN IVKYSCGSSY TKMKDQKVIK VRITDLPVGS
EEQLKENLYH QISNRYQDRV YDYMHPELLD INNSEQKNIK KTYFQFVDGF KQVEAGTVTF
EHYINEMMNN VNLLVDELMF NVEVNNNQSF FSVLTFNIKS TFKYMEENFG LEQDGNKILS
IAHLLYFKEE QEILINHPEW YSIRPRLTAF IQNHMGNVLW LAKRMLAHLS ERLDSQVLDE
DLIFISFYLN SMNIQGVKNE IKSIVLAHGY STASSMANVA NRMLKKNFFQ AIDMPIDTTI
DYIEGKVLDF IDNNSTENGL ILLVDMGSLF DLRIRLEKKI KGPLLLIDFV STPLVLEIGS
MLLQHKNIIE INEEIIKNVK INKQLVYPVE KKKKCILTCC YTGMGSAIQI QDILQKSLKQ
EDSSLAITPY DYHKLQQNKQ KELPFQIYDV VAIIGTVDPK IESVPYIGLD HLIGGEDVEA
FINILKSNFK IDEEQLKKDL IFNFSIKKII EKLTILDVNK VLNFVQDAVD KVEEKLGIKL
SNNKRFLLYL HCSCMVERIL RKEDADMQED IEEFVQREKR KIEIIGYAFS EIEKEYTIKI
SDLELRLIFD IVFSD
//