PHNF_MYCS2
ID PHNF_MYCS2 Reviewed; 244 AA.
AC A0QQ72; I7G3P0;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=HTH-type transcriptional repressor PhnF;
GN Name=phnF; OrderedLocusNames=MSMEG_0650, MSMEI_0633;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION IN REGULATION OF PHOSPHATE-UPTAKE OPERON PHNDCE, MAPPING OF
RP TRANSCRIPTIONAL START SITE, AND INDUCTION.
RX PubMed=18083811; DOI=10.1128/jb.01764-07;
RA Gebhard S., Cook G.M.;
RT "Differential regulation of high-affinity phosphate transport systems of
RT Mycobacterium smegmatis: identification of PhnF, a repressor of the phnDCE
RT operon.";
RL J. Bacteriol. 190:1335-1343(2008).
CC -!- FUNCTION: Represses the phnDCE operon, involved in the uptake of
CC phosphate, under conditions of phosphate availability in the cell.
CC {ECO:0000269|PubMed:18083811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By phosphate. {ECO:0000269|PubMed:18083811}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK72651.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AFP37114.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK72651.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP37114.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_885060.1; NC_008596.1.
DR PDB; 3F8L; X-ray; 1.90 A; A/B/C/D=76-244.
DR PDB; 3F8M; X-ray; 1.80 A; A/B=2-244.
DR PDBsum; 3F8L; -.
DR PDBsum; 3F8M; -.
DR AlphaFoldDB; A0QQ72; -.
DR SMR; A0QQ72; -.
DR STRING; 246196.MSMEI_0633; -.
DR EnsemblBacteria; ABK72651; ABK72651; MSMEG_0650.
DR EnsemblBacteria; AFP37114; AFP37114; MSMEI_0633.
DR KEGG; msg:MSMEI_0633; -.
DR KEGG; msm:MSMEG_0650; -.
DR PATRIC; fig|246196.19.peg.646; -.
DR eggNOG; COG2188; Bacteria.
DR EvolutionaryTrace; A0QQ72; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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:InterPro.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.1410.10; -; 1.
DR InterPro; IPR028978; Chorismate_lyase_/UTRA_dom_sf.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR011663; UTRA.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00392; GntR; 1.
DR Pfam; PF07702; UTRA; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00345; HTH_GNTR; 1.
DR SMART; SM00866; UTRA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF64288; SSF64288; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..244
FT /note="HTH-type transcriptional repressor PhnF"
FT /id="PRO_0000357471"
FT DOMAIN 8..74
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 35..54
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:3F8M"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:3F8M"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:3F8M"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:3F8M"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:3F8M"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:3F8M"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:3F8M"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:3F8M"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:3F8M"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:3F8M"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3F8M"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:3F8M"
SQ SEQUENCE 244 AA; 26897 MW; 49072BAD300A5A45 CRC64;
MTAGAAPRIL KHQVVRAELD RMLDGMRIGD PFPAEREIAE QFEVARETVR QALRELLIDG
RVERRGRTTV VARPKIRQPL GMGSYTEAAK AQGLSAGRIL VAWSDLTADE VLAGVLGVDV
GAPVLQLERV LTTDGVRVGL ETTKLPAQRY PGLRETFDHE ASLYAEIRSR GIAFTRTVDT
IDTALPDARE AALLGADART PMFLLNRVSY DQDDVAIEQR RSLYRGDRMT FTAVMHAKNS
AIVS
