MTLR_STRMU
ID MTLR_STRMU Reviewed; 650 AA.
AC Q02425;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative transcriptional regulator MtlR;
DE Includes:
DE RecName: Full=Putative phosphotransferase enzyme IIA component;
DE EC=2.7.1.-;
DE AltName: Full=Putative PTS system EIIA component;
GN Name=mtlR; OrderedLocusNames=SMU_1184c;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 700611 / UA130 / Serotype c;
RX PubMed=10878121; DOI=10.1099/00221287-146-7-1565;
RA Honeyman A.L., Curtiss R. III;
RT "The mannitol-specific enzyme II (mtlA) gene and the mtlR gene of the PTS
RT of Streptococcus mutans.";
RL Microbiology 146:1565-1572(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-650.
RC STRAIN=ATCC 700611 / UA130 / Serotype c;
RX PubMed=1322373; DOI=10.1128/iai.60.8.3369-3375.1992;
RA Honeyman A.L., Curtiss R. III;
RT "Isolation, characterization, and nucleotide sequence of the Streptococcus
RT mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific
RT factor III gene of the phosphoenolpyruvate phosphotransferase system.";
RL Infect. Immun. 60:3369-3375(1992).
CC -!- FUNCTION: Not necessary for mannitol utilization. May be involved in
CC regulation of the mannitol phosphoenolpyruvate-dependent sugar
CC phosphotransferase system (PTS). {ECO:0000269|PubMed:10878121}.
CC -!- DOMAIN: The PTS EIIA type-2 domain may serve a regulatory function,
CC through its phosphorylation activity.
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DR EMBL; AF210133; AAA26940.2; -; Genomic_DNA.
DR EMBL; AE014133; AAN58874.1; -; Genomic_DNA.
DR PIR; A44798; A44798.
DR RefSeq; NP_721568.1; NC_004350.2.
DR RefSeq; WP_002262166.1; NC_004350.2.
DR AlphaFoldDB; Q02425; -.
DR SMR; Q02425; -.
DR STRING; 210007.SMU_1184c; -.
DR PRIDE; Q02425; -.
DR EnsemblBacteria; AAN58874; AAN58874; SMU_1184c.
DR KEGG; smu:SMU_1184c; -.
DR PATRIC; fig|210007.7.peg.1062; -.
DR eggNOG; COG3711; Bacteria.
DR HOGENOM; CLU_013442_2_2_9; -.
DR OMA; QKIFQAY; -.
DR PhylomeDB; Q02425; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR013196; HTH_11.
DR InterPro; IPR007737; Mga_HTH.
DR InterPro; IPR011608; PRD.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF08279; HTH_11; 1.
DR Pfam; PF05043; Mga; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR PROSITE; PS51372; PRD_2; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
PE 3: Inferred from homology;
KW Kinase; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..650
FT /note="Putative transcriptional regulator MtlR"
FT /id="PRO_0000096630"
FT DOMAIN 276..382
FT /note="PRD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 490..640
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT MOD_RES 556
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT CONFLICT 361..363
FT /note="KEP -> RES (in Ref. 1; AAA26940)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="V -> A (in Ref. 1; AAA26940)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="M -> I (in Ref. 1; AAA26940)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="K -> R (in Ref. 1; AAA26940)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="C -> R (in Ref. 1; AAA26940 and 3; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="H -> R (in Ref. 1; AAA26940 and 3; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="L -> P (in Ref. 1; AAA26940 and 3; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 75338 MW; 02F1229435B7C97A CRC64;
MLLTKREKHL LAAFQNYGKL SLKQMIDLLK VSQRTVYRTI SDLTDSLNTI NISIIKENQN
YFLVGELANL ASIISLDTYE QYERLNLITY KLLMSFSSIT NEQLQEEFNV SNVTIIQDIA
EIEKRLADFD LRLDRKKGYR LVGNKNTLRR LLAILLTNNL SISDFGAGAY GHFEVLDKAK
LELAKQIFQS SQEDLPDLDA KMSEFFIILL ALSGWRDNEA VGHSISKAAL DFSQKVYTEF
SQKTNQFYSI QEILYYASIL DELVIKRQET PLFHEKFDSA FFYNISNLID KVSLYTKINF
AKDKTLFHFL FNHIRLNLAV PQIFEDKSNN TIAHEVVQGN EYLHRVVSLL VQDIFPKYLQ
KEPEYELITL HFASSLRRSP DIYPIKILLL TDERPLAREL LITRIKTIAP FVDKVVVKEL
AQYETKDKDY YNCVLATKPL VDKAVKMVST YPDAKEMLQL QDYLQNVQAH QKIIIRDEQT
NKQGYNLQNY FLATQQLLQE FSYQEIDNPA DFETSVPKIM ETIAAVSDKT YLSSKLLKCF
AVSPLAIPET HLALLHTQSS KVITSCFKIY DLKRPVTALS MNYEKETVTR ILVMLTRLDE
TKEMRDLMTA ISQSIIENHL YTEIYKTGNK DIIYQLLNQI FTEKIKKLET
