ID   RCOM2_PARXL             Reviewed;         267 AA.
AC   Q13IY4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Heme-containing CO-sensing transcriptional regulator RcoM 2;
DE   AltName: Full=Regulator of CO metabolism 2;
DE            Short=RCOM-2;
GN   Name=rcoM2; OrderedLocusNames=Bxeno_C0027; ORFNames=Bxe_C0028;
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.
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).
RN   [3]
RP   CHARACTERIZATION, AND HEME COFACTOR.
RX   PubMed=18672900; DOI=10.1021/bi800486x;
RA   Marvin K.A., Kerby R.L., Youn H., Roberts G.P., Burstyn J.N.;
RT   "The transcription regulator RcoM-2 from Burkholderia xenovorans is a
RT   cysteine-ligated hemoprotein that undergoes a redox-mediated ligand
RT   switch.";
RL   Biochemistry 47:9016-9028(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; CP000272; ABE35955.1; -; Genomic_DNA.
DR   RefSeq; WP_011493215.1; NZ_CP008761.1.
DR   AlphaFoldDB; Q13IY4; -.
DR   SMR; Q13IY4; -.
DR   STRING; 266265.Bxe_C0028; -.
DR   EnsemblBacteria; ABE35955; ABE35955; Bxe_C0028.
DR   KEGG; bxb:DR64_8397; -.
DR   KEGG; bxe:Bxe_C0028; -.
DR   PATRIC; fig|266265.5.peg.7807; -.
DR   eggNOG; COG3279; Bacteria.
DR   eggNOG; COG5000; Bacteria.
DR   OMA; IFGHIPR; -.
DR   OrthoDB; 1958442at2; -.
DR   Proteomes; UP000001817; Chromosome 3.
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; 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.
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 2"
FT                   /id="PRO_0000352734"
FT   DOMAIN          15..86
FT                   /note="PAS"
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"
SQ   SEQUENCE   267 AA;  29471 MW;  8E2A18388C715776 CRC64;
     MKSSESAAAT ASERRAETFQ HKLEQFNPGI VWLDPQGHVS AFNDVALHIL GPAGEQSLGV
     AQDHLFGIDV VQLHPEKSRD KLRFLLQSRD AGGCPVRSPP PVAMMINIPD RILMIKVSKM
     TGAAGTCGSC MIFYDVTDLT TEPSSQPAGA SVPAPRRLFK IPVYRKSRVI LIDLKDIVRF
     QGDGHYTTIV TKDERYLSNL SLADLELRLD SSVYLRVHRS HIVSLPYAVE LVKLDESVNL
     VMDDAEQTQV PVSRSRTAQL KELLGVV