ID   MECA1_ALKHC             Reviewed;         201 AA.
AC   Q9KCF1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Adapter protein MecA 1;
GN   Name=mecA1; OrderedLocusNames=BH1620;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05339.1; -; Genomic_DNA.
DR   PIR; D83852; D83852.
DR   RefSeq; WP_010897783.1; NC_002570.2.
DR   AlphaFoldDB; Q9KCF1; -.
DR   SMR; Q9KCF1; -.
DR   STRING; 272558.10174237; -.
DR   EnsemblBacteria; BAB05339; BAB05339; BAB05339.
DR   KEGG; bha:BH1620; -.
DR   eggNOG; COG4862; Bacteria.
DR   HOGENOM; CLU_071496_3_0_9; -.
DR   OMA; IEMQVKL; -.
DR   OrthoDB; 1678325at2; -.
DR   Proteomes; UP000001258; 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; 2.
DR   PIRSF; PIRSF029008; MecA; 1.
PE   3: Inferred from homology;
KW   Competence; Reference proteome; Sporulation.
FT   CHAIN           1..201
FT                   /note="Adapter protein MecA 1"
FT                   /id="PRO_0000212264"
SQ   SEQUENCE   201 AA;  22819 MW;  AA4343E1C4E2168B CRC64;
     MRLERLAVNK IKVFLTFDDL KERGITKDEL WQDIPKVHDL FRDMMLEADD ELGFKADGPI
     AVEVFALPAQ GMVIIVTKGH QESDFDEDGL EDGYIEMQVT LDESDEVFYE FADIEDVISL
     VPRLVTLGMT GGTLYSYQGR YYISFTDLDL DGIDEESLIA LLAEYGYPST ISTYRVAEYG
     SLIIANDACI KLYQSFFKAR T