ID A9IKD7_BORPD Unreviewed; 306 AA.
AC A9IKD7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=HTH-type transcriptional regulator MetR {ECO:0000256|ARBA:ARBA00019365};
GN Name=metR {ECO:0000313|EMBL:CAP42398.1};
GN OrderedLocusNames=Bpet2058 {ECO:0000313|EMBL:CAP42398.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42398.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP42398.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000256|ARBA:ARBA00009437}.
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; AM902716; CAP42398.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IKD7; -.
DR STRING; 94624.Bpet2058; -.
DR KEGG; bpt:Bpet2058; -.
DR eggNOG; COG0583; Bacteria.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08441; PBP2_MetR; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR037406; MetR_PBP2.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR30126; HTH-TYPE TRANSCRIPTIONAL REGULATOR; 1.
DR PANTHER; PTHR30126:SF25; HTH-TYPE TRANSCRIPTIONAL REGULATOR METR; 1.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 2..59
FT /note="HTH lysR-type"
FT /evidence="ECO:0000259|PROSITE:PS50931"
SQ SEQUENCE 306 AA; 33884 MW; FC5B44CC6A2F646B CRC64;
MLEIRHLETL SAIRDGGSLQ EAAERLHLTQ SALSHQLRDL ETRLGTPLLN RRTRPARLTT
AGLRVLALAD EILPRLRATE RELQKLAAGR TGRLHLAIEC HSCFQWLMPA LDAFRGQWPD
VALDLSAAFS FAPLPALVRG DLDLVITSDP LRLEAVEYLP LFKYELVLAV AGSHPLASLR
HVEPEQLADQ TLITYPVDRQ RLDVFTAFLD PAGVEPAAVR KAELTPIIAQ LVASNRGVAA
LPNWALTEYL RPGWLKLCHL GPQGVWRTLY AAVRTEDTEA SYVGDFLAIA REVCFKTLDG
IRSAKA
//
