ID   A0A1T5A4N6_9BACI        Unreviewed;       222 AA.
AC   A0A1T5A4N6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Adapter protein MecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN   Name=mecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN   ORFNames=SAMN06295926_101305 {ECO:0000313|EMBL:SKB29918.1};
OS   Lysinibacillus sp. AC-3.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1680467 {ECO:0000313|EMBL:SKB29918.1, ECO:0000313|Proteomes:UP000190941};
RN   [1] {ECO:0000313|EMBL:SKB29918.1, ECO:0000313|Proteomes:UP000190941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC-3 {ECO:0000313|EMBL:SKB29918.1,
RC   ECO:0000313|Proteomes:UP000190941};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; FUYW01000001; SKB29918.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5A4N6; -.
DR   STRING; 1680467.SAMN06295926_101305; -.
DR   Proteomes; UP000190941; 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:SF2; ADAPTER PROTEIN MECA 2; 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   Sporulation {ECO:0000256|HAMAP-Rule:MF_01124}.
SQ   SEQUENCE   222 AA;  26447 MW;  FDEBCD3A1D331882 CRC64;
     MDIERVNENT LKLFITYNDI EDRGYSREEI WYNRAKGEQL FWDMIDEVNT EDYFDVEGPI
     WIHINASEVG LEIIVTRAHI LKDGETLDGS SHFDEHKDMF APFEDVGEDL LSQLTQFGDI
     DESELFMDTD IYVYKFKDID ELIPVAKRIT DELVDSSLFK YENWYYLVVD FANAEEELNH
     HDRNAVIKEF LLPSNFTIHR LEEYGEKIME FDCFETVRKY FI
//