RCOM1_PARXL
ID RCOM1_PARXL Reviewed; 267 AA.
AC Q13YL3;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Heme-containing CO-sensing transcriptional regulator RcoM 1;
DE AltName: Full=Regulator of CO metabolism 1;
DE Short=RCOM-1;
GN Name=rcoM1; OrderedLocusNames=Bxeno_A2288; ORFNames=Bxe_A2142;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
RN [2]
RP FUNCTION IN REGULATION OF AEROBIC CO OXIDATION, HEME COFACTOR, AND
RP MUTAGENESIS OF HIS-74; MET-104; MET-105 AND HIS-218.
RX PubMed=18326575; DOI=10.1128/jb.00033-08;
RA Kerby R.L., Youn H., Roberts G.P.;
RT "RcoM: a new single-component transcriptional regulator of CO metabolism in
RT bacteria.";
RL J. Bacteriol. 190:3336-3343(2008).
CC -!- FUNCTION: One-component, b-type heme-containing aerobic sensor and
CC transcriptional regulator that responds to CO by activating the
CC expression of the oxidation operon cox. {ECO:0000269|PubMed:18326575}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The N-terminal sensor (heme-containing) domain is covalently
CC linked to the C-terminal, DNA-binding response domain.
CC -!- DOMAIN: Binding of an external ligand to the heme located in the N-
CC terminal sensory domain displaces the Met-104 distal heme ligand,
CC triggering a conformational change that activates the C-terminal DNA-
CC binding domain.
CC -!- MISCELLANEOUS: This protein undergoes a ligand switch upon reduction;
CC the heme distal ligand is coordinated by a Cys residue in the inactive
CC Fe(3+) (ferric) form, by Met-104 in the inactive Fe(2+) (ferrous) form,
CC and by CO in the CO-bound active form.
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; CP000270; ABE30826.1; -; Genomic_DNA.
DR RefSeq; WP_011488440.1; NZ_CP008760.1.
DR AlphaFoldDB; Q13YL3; -.
DR SMR; Q13YL3; -.
DR STRING; 266265.Bxe_A2142; -.
DR EnsemblBacteria; ABE30826; ABE30826; Bxe_A2142.
DR KEGG; bxb:DR64_4297; -.
DR KEGG; bxe:Bxe_A2142; -.
DR PATRIC; fig|266265.5.peg.2393; -.
DR eggNOG; COG3279; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR OMA; EGHYARA; -.
DR OrthoDB; 1958442at2; -.
DR Proteomes; UP000001817; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR007492; LytTR_DNA-bd_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR Pfam; PF04397; LytTR; 1.
DR SMART; SM00850; LytTR; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS50930; HTH_LYTTR; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Heme; Iron; Metal-binding;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..267
FT /note="Heme-containing CO-sensing transcriptional regulator
FT RcoM 1"
FT /id="PRO_0000352733"
FT DOMAIN 15..86
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 161..266
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00112"
FT BINDING 74
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 104
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MUTAGEN 74
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18326575"
FT MUTAGEN 74
FT /note="H->K: Loss of ability to bind heme. Loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:18326575"
FT MUTAGEN 74
FT /note="H->Y: Loss of ability to bind heme. Loss of ability
FT to respond to CO, presenting constitutive activity."
FT /evidence="ECO:0000269|PubMed:18326575"
FT MUTAGEN 104
FT /note="M->K: Slower binding of CO."
FT /evidence="ECO:0000269|PubMed:18326575"
FT MUTAGEN 104
FT /note="M->L: Much higher affinity for CO. Loss of activity.
FT No effect on heme incorporation."
FT /evidence="ECO:0000269|PubMed:18326575"
FT MUTAGEN 105
FT /note="M->L: No effect."
FT /evidence="ECO:0000269|PubMed:18326575"
FT MUTAGEN 218
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18326575"
SQ SEQUENCE 267 AA; 29451 MW; 79B01458570B7072 CRC64;
MKSSEPASVS AAERRAETFQ HKLEQFNPGI VWLDQHGRVT AFNDVALQIL GPAGEQSLGV
AQDSLFGIDV VQLHPEKSRD KLRFLLQSKD VGGCPVKSPP PVAMMINIPD RILMIKVSSM
IAAGGACGTC MIFYDVTDLT TEPSGLPAGG SAPSPRRLFK IPVYRKNRVI LLDLKDIVRF
QGDGHYTTIV TRDDRYLSNL SLADLELRLD SSIYLRVHRS HIVSLQYAVE LVKLDESVNL
VMDDAEQTQV PVSRSRTAQL KELLGVV
