ID   MECA2_BACCR             Reviewed;         202 AA.
AC   Q81FS9;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Adapter protein MecA 2;
GN   Name=mecA2; OrderedLocusNames=BC_1490;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- FUNCTION: Enables the recognition and targeting of unfolded and
CC       aggregated proteins to the ClpC protease or to other proteins involved
CC       in proteolysis. Acts negatively in the development of competence by
CC       binding ComK and recruiting it to the ClpCP protease. When
CC       overexpressed, inhibits sporulation. Also involved in Spx degradation
CC       by ClpC (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal domain has binding sites for ComK and probably
CC       for unfolded/aggregated proteins; the C-terminal domain interacts with
CC       ClpC.
CC   -!- SIMILARITY: Belongs to the MecA family. {ECO:0000305}.
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DR   EMBL; AE016877; AAP08470.1; -; Genomic_DNA.
DR   RefSeq; NP_831269.1; NC_004722.1.
DR   RefSeq; WP_001235402.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81FS9; -.
DR   SMR; Q81FS9; -.
DR   STRING; 226900.BC_1490; -.
DR   EnsemblBacteria; AAP08470; AAP08470; BC_1490.
DR   GeneID; 67506191; -.
DR   KEGG; bce:BC1490; -.
DR   PATRIC; fig|226900.8.peg.1467; -.
DR   HOGENOM; CLU_071496_3_0_9; -.
DR   OMA; IEMQVKL; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0045808; P:negative regulation of establishment of competence for transformation; IEA:UniProtKB-UniRule.
DR   GO; GO:0042174; P:negative regulation of sporulation resulting in formation of a cellular spore; IEA:UniProtKB-UniRule.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.1950; -; 1.
DR   HAMAP; MF_01124; MecA; 1.
DR   InterPro; IPR038471; MecA_C_sf.
DR   InterPro; IPR008681; Neg-reg_MecA.
DR   PANTHER; PTHR39161; PTHR39161; 1.
DR   Pfam; PF05389; MecA; 1.
DR   PIRSF; PIRSF029008; MecA; 1.
PE   3: Inferred from homology;
KW   Competence; Reference proteome; Sporulation.
FT   CHAIN           1..202
FT                   /note="Adapter protein MecA 2"
FT                   /id="PRO_0000212263"
SQ   SEQUENCE   202 AA;  23791 MW;  EE1E12B35D5FCA3A CRC64;
     MRLERLNYNK IKIFLTFDDL SERGLTKEDL WRNAPKVQQL FRDMMQEANK ELGFEADGPI
     AVEVFSLQAQ GMVVIVTKEN QEMDTDDEFR DEFIEMQVTL DESEHILYEF ATLDDVINLS
     NRLYNLGVTG GKLYTWDERF YLWVEEEEQI QLLKADFIAI LAEYGNPSTA TIYRIMEYGK
     ELMDVNAIEQ IHNYFVKKQN LS