FADR_VIBCH
ID FADR_VIBCH Reviewed; 279 AA.
AC Q9KQU8;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Fatty acid metabolism regulator protein {ECO:0000255|HAMAP-Rule:MF_00696};
GN Name=fadR {ECO:0000255|HAMAP-Rule:MF_00696}; OrderedLocusNames=VC_1900;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12562793; DOI=10.1128/jb.185.4.1236-1244.2003;
RA Herz K., Vimont S., Padan E., Berche P.;
RT "Roles of NhaA, NhaB, and NhaD Na(+)/H(+) antiporters in survival of Vibrio
RT cholerae in a saline environment.";
RL J. Bacteriol. 185:1236-1244(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Multifunctional regulator of fatty acid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00696}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00696}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00696}.
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; AF489522; AAO37924.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95048.1; -; Genomic_DNA.
DR PIR; B82144; B82144.
DR RefSeq; NP_231534.1; NC_002505.1.
DR RefSeq; WP_000234820.1; NZ_LT906614.1.
DR PDB; 4P9U; X-ray; 3.21 A; A/B/E/F=6-277.
DR PDB; 4PDK; X-ray; 2.80 A; A/B=1-279.
DR PDBsum; 4P9U; -.
DR PDBsum; 4PDK; -.
DR AlphaFoldDB; Q9KQU8; -.
DR SMR; Q9KQU8; -.
DR STRING; 243277.VC_1900; -.
DR DNASU; 2613529; -.
DR EnsemblBacteria; AAF95048; AAF95048; VC_1900.
DR GeneID; 57740533; -.
DR KEGG; vch:VC_1900; -.
DR PATRIC; fig|243277.26.peg.1816; -.
DR eggNOG; COG2186; Bacteria.
DR HOGENOM; CLU_017584_9_4_6; -.
DR OMA; WETAGPN; -.
DR BioCyc; VCHO:VC1900-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; IMP:CACAO.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.120.530; -; 1.
DR HAMAP; MF_00696; HTH_FadR; 1.
DR InterPro; IPR014178; FA-response_TF_FadR.
DR InterPro; IPR028374; FadR_C.
DR InterPro; IPR008920; TF_FadR/GntR_C.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR43537:SF10; PTHR43537:SF10; 1.
DR Pfam; PF07840; FadR_C; 1.
DR Pfam; PF00392; GntR; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48008; SSF48008; 1.
DR TIGRFAMs; TIGR02812; fadR_gamma; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Fatty acid metabolism;
KW Lipid metabolism; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..279
FT /note="Fatty acid metabolism regulator protein"
FT /id="PRO_0000050636"
FT DOMAIN 6..74
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00696"
FT DNA_BIND 34..53
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00696"
FT HELIX 9..21
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:4PDK"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4P9U"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4PDK"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4PDK"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4PDK"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 97..119
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 121..139
FT /evidence="ECO:0007829|PDB:4PDK"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 169..194
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 223..242
FT /evidence="ECO:0007829|PDB:4PDK"
FT HELIX 248..263
FT /evidence="ECO:0007829|PDB:4PDK"
SQ SEQUENCE 279 AA; 31998 MW; 47D710A53CC4F5B1 CRC64;
MVIKAKSPAG FAEKYIIESI WNGRFPPGSI LPAERELSEL IGVTRTTLRE VLQRLARDGW
LTIQHGKPTK VNQFMETSGL HILDTLMTLD AENATSIVED LLAARTNISP IFMRYAFKLN
KESAERIMIN VIESCEALVN APSWDAFIAA SPYAEKIQQH VKEDSEKDEL KRQEILIAKT
FNFYDYMLFQ RLAFHSGNQI YGLIFNGLKK LYDRVGSYYF SNPQARELAM EFYRQLLAVC
QSGEREHLPQ VIRQYGIASG HIWNQMKMTL PSNFTEDDC