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 03-AUG-2022, entry version 163.
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; Moraxellales; Moraxellaceae;
OC 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 gene
RT 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 catechol
RT 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., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11932465; DOI=10.1099/00221287-148-4-1213;
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; DOI=10.1107/s0907444903021589;
RA Clark T.J., Haddad S., Neidle E.L., Momany C.;
RT "Crystallization of the effector-binding domains of BenM and CatM, LysR-
RT 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 and
CC benPK in response to cis,cis-muconate. It binds to the catB-catM
CC intercistronic region, to a specific sequence upstream of catA and to
CC 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 investigations
CC have shown it to be a transcriptional activator.
CC {ECO:0000305|PubMed:2793826}.
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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 AlphaFoldDB; P07774; -.
DR SMR; P07774; -.
DR STRING; 62977.ACIAD1445; -.
DR EnsemblBacteria; CAG68308; CAG68308; ACIAD1445.
DR GeneID; 45233857; -.
DR KEGG; aci:ACIAD1445; -.
DR eggNOG; COG0583; Bacteria.
DR HOGENOM; CLU_039613_6_4_6; -.
DR OMA; YKYALQM; -.
DR OrthoDB; 1439189at2; -.
DR BioCyc; ASP62977:ACIAD_RS06675-MON; -.
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;
KW 3D-structure; Activator; Aromatic hydrocarbons catabolism; DNA-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..303
FT /note="HTH-type transcriptional regulator CatM"
FT /id="PRO_0000105599"
FT DOMAIN 1..58
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 18..37
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT BINDING 99
FT /ligand="cis,cis-muconate"
FT /ligand_id="ChEBI:CHEBI:32379"
FT /evidence="ECO:0000269|PubMed:17291527"
FT BINDING 128
FT /ligand="cis,cis-muconate"
FT /ligand_id="ChEBI:CHEBI:32379"
FT /evidence="ECO:0000269|PubMed:17291527"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2H98"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2H98"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:2H98"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:2H98"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:2H98"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2H98"
FT STRAND 154..169
FT /evidence="ECO:0007829|PDB:2H98"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:2H98"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3GLB"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:2H98"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2H98"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:2H98"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:2H98"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2H98"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:2H98"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:2H98"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:2H98"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:2H98"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:2H98"
FT HELIX 281..295
FT /evidence="ECO:0007829|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
