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Database: UniProt
Entry: F4BS12_CARS1
LinkDB: F4BS12_CARS1
Original site: F4BS12_CARS1 
ID   F4BS12_CARS1            Unreviewed;       698 AA.
AC   F4BS12;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Transcriptional regulator MtlR {ECO:0000313|EMBL:AEB30082.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:AEB30082.1};
DE            EC=2.7.1.69 {ECO:0000313|EMBL:AEB30082.1};
GN   Name=mtlR1 {ECO:0000313|EMBL:AEB30082.1};
GN   OrderedLocusNames=CAR_c14210 {ECO:0000313|EMBL:AEB30082.1};
OS   Carnobacterium sp. (strain 17-4).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=208596 {ECO:0000313|EMBL:AEB30082.1, ECO:0000313|Proteomes:UP000008304};
RN   [1] {ECO:0000313|EMBL:AEB30082.1, ECO:0000313|Proteomes:UP000008304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17-4 {ECO:0000313|EMBL:AEB30082.1,
RC   ECO:0000313|Proteomes:UP000008304};
RX   PubMed=21551290; DOI=10.1128/JB.05113-11;
RA   Voget S., Klippel B., Daniel R., Antranikian G.;
RT   "Complete gnome sequence of Carnobacterium sp. 17-4.";
RL   J. Bacteriol. 193:3403-3404(2011).
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DR   EMBL; CP002563; AEB30082.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4BS12; -.
DR   STRING; 208596.CAR_c14210; -.
DR   KEGG; crn:CAR_c14210; -.
DR   eggNOG; COG1762; Bacteria.
DR   eggNOG; COG3711; Bacteria.
DR   HOGENOM; CLU_013442_2_0_9; -.
DR   OrthoDB; 9776005at2; -.
DR   Proteomes; UP000008304; Chromosome.
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; cd05568; PTS_IIB_bgl_like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.1790.10; PRD domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR007737; Mga_HTH.
DR   InterPro; IPR011608; PRD.
DR   InterPro; IPR036634; PRD_sf.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR30185; CRYPTIC BETA-GLUCOSIDE BGL OPERON ANTITERMINATOR; 1.
DR   PANTHER; PTHR30185:SF18; TRANSCRIPTIONAL REGULATOR MTLR; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   Pfam; PF05043; Mga; 1.
DR   Pfam; PF00874; PRD; 2.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR   SUPFAM; SSF63520; PTS-regulatory domain, PRD; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51372; PRD_2; 2.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008304};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEB30082.1}.
FT   DOMAIN          202..309
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          314..420
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          423..512
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          545..691
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   698 AA;  80269 MW;  7B912EC57B76CB1C CRC64;
     MKELYISNRE KKIIEILLEQ KNGVSLDYLS DELQVSNRTI YRELSSLEST LAQYQIKLIR
     ELDIGYRLVG KPALFRELQQ QLYASPEEFT AQQRQSALVI KLLTQENEVK MESLAIDLQV
     SISTIQADLV SIEEVFKAYQ IDIERKKAKG IQAMASESNR RLIISGLIHS EINEYDFFQL
     LENETKAQDK EWGNGQNPFL KQLTKEDLYH VYAVVKQFGQ HYFDEVTDSQ LQRLVILLCV
     SIMRLREGYQ ITSFKTNTFL TDSNQTKSLE TATAIYEFMQ KLYGMTIPKE EIQFLGLQIQ
     GLNVPLRNDF FSQEYDADLG YKVRELIQLV SNEMDWNFNQ DETLFHDLLA HITAALKRAI
     APMPESNNPL LDKISTQYSQ LSFSVKENLT HIFPLIHFLP NEIVYIVIHF ASAYERQPKI
     QELKALVICS SGVGTAKILE SRIRKHIPEI TVIEISRISK LHRIDFNEYD LILSTIFLQG
     FETEYKVVTP LLMDNEIKSI QLYVRQIINE KIKGKVRKET LVLTTPQTDK SEFKEFYQKL
     TLANGVLENF DLHQTIGMMD LNSIISAICE SLEGEFLTDG KHVATKLMER MELAPIGLPN
     TNMALFHCID ATIKQPFFSI YELPNTMDVL GIDRNPVHMK RVLMMLGPDP LSENAQEILG
     FISSAIVESD LTMEIFNSGS EPLLNNYLSG LFLEKLKK
//
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