ID   CARD_MYCTU              Reviewed;         162 AA.
AC   P9WJG3; F2GJS9; L0TFY0; O53568; Q7D585;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=RNA polymerase-binding transcription factor CarD;
GN   Name=carD; OrderedLocusNames=Rv3583c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Erdman;
RX   PubMed=19596241; DOI=10.1016/j.cell.2009.04.041;
RA   Stallings C.L., Stephanou N.C., Chu L., Hochschild A., Nickels B.E.,
RA   Glickman M.S.;
RT   "CarD is an essential regulator of rRNA transcription required for
RT   Mycobacterium tuberculosis persistence.";
RL   Cell 138:146-159(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [4]
RP   FUNCTION, INTERACTION WITH RPOB, AND MUTAGENESIS OF ARG-25 AND ARG-47.
RC   STRAIN=Erdman;
RX   PubMed=22904282; DOI=10.1128/jb.00879-12;
RA   Weiss L.A., Harrison P.G., Nickels B.E., Glickman M.S., Campbell E.A.,
RA   Darst S.A., Stallings C.L.;
RT   "Interaction of CarD with RNA polymerase mediates Mycobacterium
RT   tuberculosis viability, rifampicin resistance, and pathogenesis.";
RL   J. Bacteriol. 194:5621-5631(2012).
CC   -!- FUNCTION: Controls rRNA transcription by binding to the RNA polymerase
CC       (RNAP). Required for replication and persistence during infection of
CC       mice. {ECO:0000269|PubMed:19596241, ECO:0000269|PubMed:22904282}.
CC   -!- SUBUNIT: Interacts directly with the N-terminus of the RNA polymerase
CC       subunit beta (RpoB). {ECO:0000269|PubMed:22904282}.
CC   -!- INTERACTION:
CC       P9WJG3; P9WGY9: rpoB; NbExp=5; IntAct=EBI-6421028, EBI-6419676;
CC   -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted.
CC       {ECO:0000269|PubMed:19596241}.
CC   -!- SIMILARITY: Belongs to the CarD family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP46406.1; -; Genomic_DNA.
DR   PIR; H70803; H70803.
DR   RefSeq; NP_218100.1; NC_000962.3.
DR   RefSeq; WP_003419482.1; NZ_NVQJ01000014.1.
DR   PDB; 4ILU; X-ray; 2.30 A; A=1-162.
DR   PDB; 4KBM; X-ray; 2.11 A; B=1-162.
DR   PDB; 4KMC; X-ray; 2.15 A; A=83-162.
DR   PDB; 4MFR; X-ray; 2.50 A; A=1-162.
DR   PDB; 6EDT; EM; -; M=1-162.
DR   PDB; 6EE8; EM; 3.92 A; M=1-162.
DR   PDB; 6EEC; EM; 3.55 A; M=1-162.
DR   PDB; 6VVX; EM; 3.39 A; M=1-162.
DR   PDB; 6VVY; EM; 3.42 A; M=1-162.
DR   PDB; 6VVZ; EM; 3.72 A; M=1-162.
DR   PDB; 6VW0; EM; 3.59 A; M=1-162.
DR   PDB; 7KIF; EM; 2.94 A; M=1-162.
DR   PDB; 7KIM; EM; 3.38 A; M=1-162.
DR   PDB; 7KIN; EM; 2.74 A; M=1-162.
DR   PDBsum; 4ILU; -.
DR   PDBsum; 4KBM; -.
DR   PDBsum; 4KMC; -.
DR   PDBsum; 4MFR; -.
DR   PDBsum; 6EDT; -.
DR   PDBsum; 6EE8; -.
DR   PDBsum; 6EEC; -.
DR   PDBsum; 6VVX; -.
DR   PDBsum; 6VVY; -.
DR   PDBsum; 6VVZ; -.
DR   PDBsum; 6VW0; -.
DR   PDBsum; 7KIF; -.
DR   PDBsum; 7KIM; -.
DR   PDBsum; 7KIN; -.
DR   AlphaFoldDB; P9WJG3; -.
DR   SMR; P9WJG3; -.
DR   IntAct; P9WJG3; 7.
DR   STRING; 83332.Rv3583c; -.
DR   PaxDb; P9WJG3; -.
DR   DNASU; 887854; -.
DR   GeneID; 64258344; -.
DR   GeneID; 66743455; -.
DR   GeneID; 887854; -.
DR   KEGG; mtu:Rv3583c; -.
DR   TubercuList; Rv3583c; -.
DR   eggNOG; COG1329; Bacteria.
DR   OMA; DMKVMIP; -.
DR   PhylomeDB; P9WJG3; -.
DR   PHI-base; PHI:7578; -.
DR   PRO; PR:P9WJG3; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009303; P:rRNA transcription; IDA:MTBBASE.
DR   GO; GO:0015968; P:stringent response; IBA:GO_Central.
DR   Gene3D; 1.20.58.1290; -; 1.
DR   InterPro; IPR036101; CarD-like/TRCF_dom_sf.
DR   InterPro; IPR003711; CarD-like/TRCF_domain.
DR   InterPro; IPR042215; CarD-like_C.
DR   Pfam; PF02559; CarD_CdnL_TRCF; 1.
DR   SMART; SM01058; CarD_TRCF; 1.
DR   SUPFAM; SSF141259; SSF141259; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Virulence.
FT   CHAIN           1..162
FT                   /note="RNA polymerase-binding transcription factor CarD"
FT                   /id="PRO_0000420262"
FT   MUTAGEN         25
FT                   /note="R->E: Weakens interaction with RpoB. Abolishes
FT                   interaction with RpoB; when associated with E-47."
FT                   /evidence="ECO:0000269|PubMed:22904282"
FT   MUTAGEN         47
FT                   /note="R->E: Weakens interaction with RpoB, decreases
FT                   growth rate and virulence, and increases rifampicin
FT                   sensitivity. Abolishes interaction with RpoB; when
FT                   associated with E-25."
FT                   /evidence="ECO:0000269|PubMed:22904282"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:7KIM"
FT   STRAND          8..11
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   TURN            12..14
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   STRAND          15..25
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   STRAND          32..39
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   TURN            40..43
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   TURN            53..57
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:4ILU"
FT   HELIX           64..75
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   HELIX           86..97
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   HELIX           101..115
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   HELIX           122..142
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:4KBM"
FT   HELIX           150..159
FT                   /evidence="ECO:0007829|PDB:4KBM"
SQ   SEQUENCE   162 AA;  17907 MW;  15F27E0732FD6AD7 CRC64;
     MIFKVGDTVV YPHHGAALVE AIETRTIKGE QKEYLVLKVA QGDLTVRVPA ENAEYVGVRD
     VVGQEGLDKV FQVLRAPHTE EPTNWSRRYK ANLEKLASGD VNKVAEVVRD LWRRDQERGL
     SAGEKRMLAK ARQILVGELA LAESTDDAKA ETILDEVLAA AS