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Database: UniProt
Entry: F5L7S8_CALTT
LinkDB: F5L7S8_CALTT
Original site: F5L7S8_CALTT 
ID   F5L7S8_CALTT            Unreviewed;       195 AA.
AC   F5L7S8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Transcription factor FapR {ECO:0000256|HAMAP-Rule:MF_01814};
DE   AltName: Full=Fatty acid and phospholipid biosynthesis regulator {ECO:0000256|HAMAP-Rule:MF_01814};
GN   Name=fapR {ECO:0000256|HAMAP-Rule:MF_01814,
GN   ECO:0000313|EMBL:QZT32810.1};
GN   ORFNames=CathTA2_1885 {ECO:0000313|EMBL:EGL82594.1}, HUR95_10535
GN   {ECO:0000313|EMBL:QZT32810.1};
OS   Caldalkalibacillus thermarum (strain TA2.A1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX   NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL82594.1, ECO:0000313|Proteomes:UP000010716};
RN   [1] {ECO:0000313|EMBL:EGL82594.1, ECO:0000313|Proteomes:UP000010716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL82594.1,
RC   ECO:0000313|Proteomes:UP000010716};
RX   PubMed=21685297; DOI=10.1128/JB.05035-11;
RA   Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., Stockwell P.,
RA   Black M.A., Klingeman D.M., Land M.L., Han C.S., Martin S.L., Becher S.A.,
RA   Peddie C.J., Morgan H.W., Matthies D., Preiss L., Meier T., Brown S.D.,
RA   Cook G.M.;
RT   "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus
RT   thermarum strain TA2.A1.";
RL   J. Bacteriol. 193:4290-4291(2011).
RN   [2] {ECO:0000313|EMBL:QZT32810.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT32810.1};
RX   PubMed=33030592;
RA   de Jong S.I., van den Broek M.A., Merkel A.Y., de la Torre Cortes P.,
RA   Kalamorz F., Cook G.M., van Loosdrecht M.C.M., McMillan D.G.G.;
RT   "Genomic analysis of Caldalkalibacillus thermarum TA2.A1 reveals aerobic
RT   alkaliphilic metabolism and evolutionary hallmarks linking alkaliphilic
RT   bacteria and plant life.";
RL   Extremophiles 24:923-935(2020).
RN   [3] {ECO:0000313|EMBL:QZT32810.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT32810.1};
RA   de Jong S., van den Broek M., Merkel A., de la Torre Cortes P.,
RA   Kalamorz F., Cook G., van Loosdrecht M., McMillan D.;
RL   Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional factor involved in regulation of membrane
CC       lipid biosynthesis by repressing genes involved in fatty acid and
CC       phospholipid metabolism. {ECO:0000256|HAMAP-Rule:MF_01814}.
CC   -!- SIMILARITY: Belongs to the FapR family. {ECO:0000256|HAMAP-
CC       Rule:MF_01814}.
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DR   EMBL; AFCE01000144; EGL82594.1; -; Genomic_DNA.
DR   EMBL; CP082237; QZT32810.1; -; Genomic_DNA.
DR   RefSeq; WP_007505042.1; NZ_CP082237.1.
DR   AlphaFoldDB; F5L7S8; -.
DR   KEGG; cthu:HUR95_10535; -.
DR   eggNOG; COG1349; Bacteria.
DR   OrthoDB; 1706183at2; -.
DR   Proteomes; UP000010716; Unassembled WGS sequence.
DR   Proteomes; UP000825179; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03440; hot_dog; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_01814; Transcrip_fact_FapR; 1.
DR   InterPro; IPR001034; DeoR_HTH.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR006683; Thioestr_dom.
DR   InterPro; IPR017275; Transcription_factor_FapR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF03061; 4HBT; 1.
DR   Pfam; PF08220; HTH_DeoR; 1.
DR   PIRSF; PIRSF037733; Transcription_factor_FapR; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01814};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01814};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01814};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01814};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01814};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010716};
KW   Repressor {ECO:0000256|HAMAP-Rule:MF_01814};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01814};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01814}.
FT   DOMAIN          9..42
FT                   /note="HTH deoR-type"
FT                   /evidence="ECO:0000259|Pfam:PF08220"
FT   DOMAIN          114..173
FT                   /note="Thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF03061"
SQ   SEQUENCE   195 AA;  22173 MW;  869F1891F550BF7A CRC64;
     MPKLTKKERQ NQLVALLHKN PFMTDEELAR HFQVSVQTIR LDRLEKSIPE LRERIKSVAE
     QNYDEVRSLL MDEVIGEIID LHLDKSAISI LDIREEHVFT RNQIARGHHL FAQANSLAVA
     VIDDELALTA SAKIRFHRPV KVGDRVVAKA KVLETKGDRT KVQVESFCGE EMVFSGQFTV
     FRSNTNSARE VSPGT
//
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