ID   A0A1H1EKX4_9BACI        Unreviewed;       238 AA.
AC   A0A1H1EKX4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Adapter protein MecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN   Name=mecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN   ORFNames=SAMN05216231_2915 {ECO:0000313|EMBL:SDQ88796.1};
OS   Virgibacillus salinus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=553311 {ECO:0000313|EMBL:SDQ88796.1, ECO:0000313|Proteomes:UP000199444};
RN   [1] {ECO:0000313|EMBL:SDQ88796.1, ECO:0000313|Proteomes:UP000199444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10449 {ECO:0000313|EMBL:SDQ88796.1,
RC   ECO:0000313|Proteomes:UP000199444};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_01124}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01124}.
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. {ECO:0000256|HAMAP-Rule:MF_01124}.
CC   -!- SIMILARITY: Belongs to the MecA family. {ECO:0000256|ARBA:ARBA00005397,
CC       ECO:0000256|HAMAP-Rule:MF_01124}.
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; FNKD01000003; SDQ88796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1EKX4; -.
DR   STRING; 553311.SAMN05216231_2915; -.
DR   Proteomes; UP000199444; Unassembled WGS sequence.
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; ADAPTER PROTEIN MECA; 1.
DR   PANTHER; PTHR39161:SF1; ADAPTER PROTEIN MECA; 1.
DR   Pfam; PF05389; MecA; 1.
DR   PIRSF; PIRSF029008; MecA; 1.
PE   3: Inferred from homology;
KW   Competence {ECO:0000256|HAMAP-Rule:MF_01124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199444};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_01124}.
FT   REGION          110..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   238 AA;  28315 MW;  D52ED5F52364B130 CRC64;
     MEIERINENT VKFYISYIDI EDRGFEREEI WYNRERSEQL FWQMMDEVNY KEDFNVEGPL
     WIQVQALDKG LEIVVTKAQV SKNGENIELP TENGKTIDIS VDDKIEDMLD DKFGEGDENS
     SKSKKEEDED GNLSLSVMFN DFEDVIQLSH YFQDNKDKTD KIEDTLFHYD NKYYLYIEFP
     QDEEIKDEHQ EDLISQIFEF ANDTEVTIHF LEEYGKQIFA DNTFEQVRSH FPAIIGRS
//