(data stored in ACNUC15324 zone)

SWISSPROT: CATM_ACIAD

ID   CATM_ACIAD              Reviewed;         303 AA.
AC   P07774; Q43930;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 3.
DT   08-MAY-2019, entry version 145.
DE   RecName: Full=HTH-type transcriptional regulator CatM;
DE   AltName: Full=Cat operon transcriptional regulator;
GN   Name=catM; Synonyms=catR; OrderedLocusNames=ACIAD1445;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2793826; DOI=10.1128/jb.171.10.5410-5421.1989;
RA   Neidle E.L., Hartnett C., Ornston L.N.;
RT   "Characterization of Acinetobacter calcoaceticus catM, a repressor
RT   gene homologous in sequence to transcriptional activator genes.";
RL   J. Bacteriol. 171:5410-5421(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, FUNCTION, AND
RP   AUTOREGULATION.
RX   PubMed=7592340; DOI=10.1128/jb.177.20.5891-5898.1995;
RA   Romero-Arroyo C.E., Schell M.A., Gaines G.L. III, Neidle E.L.;
RT   "catM encodes a LysR-type transcriptional activator regulating
RT   catechol degradation in Acinetobacter calcoaceticus.";
RL   J. Bacteriol. 177:5891-5898(1995).
RN   [3]
RP   SEQUENCE REVISION TO 274.
RA   Collier L.S., Neidle E.L.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=11932465;
RA   Clark T.J., Momany C., Neidle E.L.;
RT   "The benPK operon, proposed to play a role in transport, is part of a
RT   regulon for benzoate catabolism in Acinetobacter sp. strain ADP1.";
RL   Microbiology 148:1213-1223(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=12620848; DOI=10.1128/AEM.69.3.1598-1606.2003;
RA   Brzostowicz P.C., Reams A.B., Clark T.J., Neidle E.L.;
RT   "Transcriptional cross-regulation of the catechol and protocatechuate
RT   branches of the beta-ketoadipate pathway contributes to carbon source-
RT   dependent expression of the Acinetobacter sp. strain ADP1 pobA gene.";
RL   Appl. Environ. Microbiol. 69:1598-1606(2003).
RN   [7]
RP   CRYSTALLIZATION.
RX   PubMed=14684899;
RA   Clark T.J., Haddad S., Neidle E.L., Momany C.;
RT   "Crystallization of the effector-binding domains of BenM and CatM,
RT   LysR-type transcriptional regulators from Acinetobacter sp. ADP1.";
RL   Acta Crystallogr. D 60:105-108(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 81-303 IN COMPLEX WITH
RP   CIS,CIS-MUCONATE, AND FUNCTION.
RX   PubMed=17291527; DOI=10.1016/j.jmb.2006.09.090;
RA   Ezezika O.C., Haddad S., Clark T.J., Neidle E.L., Momany C.;
RT   "Distinct effector-binding sites enable synergistic transcriptional
RT   activation by BenM, a LysR-type regulator.";
RL   J. Mol. Biol. 367:616-629(2007).
CC   -!- FUNCTION: Positively regulates the expression of catA, catBCIJFD
CC       and benPK in response to cis,cis-muconate. It binds to the catB-
CC       catM intercistronic region, to a specific sequence upstream of
CC       catA and to the benPK promoter region. Can also repress pca genes.
CC       {ECO:0000269|PubMed:11932465, ECO:0000269|PubMed:12620848,
CC       ECO:0000269|PubMed:17291527, ECO:0000269|PubMed:7592340}.
CC   -!- SUBUNIT: Homotetramer in solution. {ECO:0000269|PubMed:11932465,
CC       ECO:0000269|PubMed:17291527}.
CC   -!- INDUCTION: Negatively autoregulated.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:2793826) reported to be a
CC       transcriptional repressor of cat genes. However, further
CC       investigations have shown it to be a transcriptional activator.
CC       {ECO:0000305|PubMed:2793826}.
DR   EMBL; AF009224; AAC46429.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68308.1; -; Genomic_DNA.
DR   RefSeq; WP_004925462.1; NC_005966.1.
DR   PDB; 2F7B; X-ray; 1.90 A; A=81-303.
DR   PDB; 2F7C; X-ray; 2.16 A; A=81-303.
DR   PDB; 2H98; X-ray; 1.80 A; A/B=1-303.
DR   PDB; 3GLB; X-ray; 2.80 A; A/B/C/D=89-303.
DR   PDBsum; 2F7B; -.
DR   PDBsum; 2F7C; -.
DR   PDBsum; 2H98; -.
DR   PDBsum; 3GLB; -.
DR   SMR; P07774; -.
DR   STRING; 62977.ACIAD1445; -.
DR   EnsemblBacteria; CAG68308; CAG68308; ACIAD1445.
DR   KEGG; aci:ACIAD1445; -.
DR   eggNOG; ENOG4108KB2; Bacteria.
DR   eggNOG; ENOG410XSY7; LUCA.
DR   HOGENOM; HOG000233514; -.
DR   KO; K21756; -.
DR   OMA; PNIMFEG; -.
DR   OrthoDB; 1439189at2; -.
DR   BioCyc; ASP62977:ACIAD_RS06675-MONOMER; -.
DR   EvolutionaryTrace; P07774; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   PRINTS; PR00039; HTHLYSR.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P07774.
DR   SWISS-2DPAGE; P07774.
KW   3D-structure; Activator; Aromatic hydrocarbons catabolism;
KW   Complete proteome; DNA-binding; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    303       HTH-type transcriptional regulator CatM.
FT                                /FTId=PRO_0000105599.
FT   DOMAIN        1     58       HTH lysR-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00253}.
FT   DNA_BIND     18     37       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00253}.
FT   BINDING      99     99       Cis,cis-muconate.
FT                                {ECO:0000269|PubMed:17291527}.
FT   BINDING     128    128       Cis,cis-muconate.
FT                                {ECO:0000269|PubMed:17291527}.
FT   STRAND       91     96       {ECO:0000244|PDB:2H98}.
FT   HELIX        98    102       {ECO:0000244|PDB:2H98}.
FT   HELIX       105    115       {ECO:0000244|PDB:2H98}.
FT   STRAND      119    125       {ECO:0000244|PDB:2H98}.
FT   HELIX       128    136       {ECO:0000244|PDB:2H98}.
FT   STRAND      141    147       {ECO:0000244|PDB:2H98}.
FT   STRAND      154    169       {ECO:0000244|PDB:2H98}.
FT   HELIX       173    177       {ECO:0000244|PDB:2H98}.
FT   TURN        178    180       {ECO:0000244|PDB:3GLB}.
FT   HELIX       184    187       {ECO:0000244|PDB:2H98}.
FT   STRAND      192    194       {ECO:0000244|PDB:2H98}.
FT   STRAND      198    202       {ECO:0000244|PDB:2H98}.
FT   HELIX       203    213       {ECO:0000244|PDB:2H98}.
FT   STRAND      221    223       {ECO:0000244|PDB:2H98}.
FT   HELIX       227    235       {ECO:0000244|PDB:2H98}.
FT   STRAND      240    244       {ECO:0000244|PDB:2H98}.
FT   HELIX       245    249       {ECO:0000244|PDB:2H98}.
FT   STRAND      255    260       {ECO:0000244|PDB:2H98}.
FT   STRAND      266    274       {ECO:0000244|PDB:2H98}.
FT   HELIX       281    295       {ECO:0000244|PDB:2H98}.
SQ   SEQUENCE   303 AA;  34084 MW;  658BB1FF4682BB38 CRC64;
     MELRHLRYFV TVVEEQSISK AAEKLCIAQP PLSRQIQKLE EELGIQLFER GFRPAKVTEA
     GMFFYQHAVQ ILTHTAQASS MAKRIATVSQ TLRIGYVSSL LYGLLPEIIY LFRQQNPEIH
     IELIECGTKD QINALKQGKI DLGFGRLKIT DPAIRRIVLH KEQLKLAIHK HHHLNQFAAT
     GVHLSQIIDE PMLLYPVSQK PNFATFIQSL FTELGLVPSK LTEIREIQLA LGLVAAGEGV
     CIVPASAMDI GVKNLLYIPI LDDDAYSPIS LAVRNMDHSN YIPKILACVQ EVFATHHIRP
     LIE
//

If you have problems or comments...

PBIL Back to PBIL home page