ID A0A1S2QQX3_9BACI Unreviewed; 223 AA.
AC A0A1S2QQX3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Adapter protein MecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN Name=mecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN ORFNames=BIV59_19740 {ECO:0000313|EMBL:OIK08552.1};
OS Bacillus sp. MUM 13.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678001 {ECO:0000313|EMBL:OIK08552.1, ECO:0000313|Proteomes:UP000180199};
RN [1] {ECO:0000313|EMBL:OIK08552.1, ECO:0000313|Proteomes:UP000180199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 13 {ECO:0000313|EMBL:OIK08552.1,
RC ECO:0000313|Proteomes:UP000180199};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Bacillus sp. MUM 13.";
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIK08552.1}.
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; MLYQ01000103; OIK08552.1; -; Genomic_DNA.
DR RefSeq; WP_071353176.1; NZ_MLYQ01000103.1.
DR AlphaFoldDB; A0A1S2QQX3; -.
DR Proteomes; UP000180199; 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|ARBA:ARBA00023287, ECO:0000256|HAMAP-
KW Rule:MF_01124}; Reference proteome {ECO:0000313|Proteomes:UP000180199};
KW Sporulation {ECO:0000256|HAMAP-Rule:MF_01124}.
SQ SEQUENCE 223 AA; 26682 MW; 12969FA418136233 CRC64;
MEIERINDDT VKFYISYIDI EERGFDREEI WYSRERSEEL FWEMMDEVHQ EEEFMIEGPL
WIQVQALEKG LEVLVTKAQL TKDGQKIELP LTDEKMKDLP VDEKIESLLD QHFHGKQQEY
STVQFEDGFI EFITEFKDFE DLIALSERSG LEGLNTKLYA YGDKYFLYIE FSEEDIEEEE
IDNILSILLE YSEESPITVH MLQEYGKVVM ENDVFDTVYK YFS
//
