ID A0A1B1Z3P6_9BACI Unreviewed; 223 AA.
AC A0A1B1Z3P6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Adapter protein MecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN Name=mecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN ORFNames=ABE41_008565 {ECO:0000313|EMBL:ANX12058.1};
OS Fictibacillus arsenicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX12058.1, ECO:0000313|Proteomes:UP000077412};
RN [1] {ECO:0000313|EMBL:ANX12058.1, ECO:0000313|Proteomes:UP000077412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-54 {ECO:0000313|EMBL:ANX12058.1,
RC ECO:0000313|Proteomes:UP000077412};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain with
RT toxicity to nematodes and a potential arsenic-resistance activity.";
RL Submitted (AUG-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}.
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DR EMBL; CP016761; ANX12058.1; -; Genomic_DNA.
DR RefSeq; WP_066288823.1; NZ_CP016761.1.
DR AlphaFoldDB; A0A1B1Z3P6; -.
DR STRING; 255247.ABE41_008565; -.
DR KEGG; far:ABE41_008565; -.
DR OrthoDB; 2360201at2; -.
DR Proteomes; UP000077412; 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; 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:UP000077412};
KW Sporulation {ECO:0000256|HAMAP-Rule:MF_01124}.
SQ SEQUENCE 223 AA; 26352 MW; 0C68140FBE553B32 CRC64;
MEIERVNEFT IKFFITYRDI EDRGFDREEI WADRERGEEL FWEMMDEAHQ QEQFPLEGPL
WIQVQALDKG LEIIVTRAQM SKDGKKIELP IGDDKLDLPV DQNIEKLLDQ QFQSEEEEFD
ELEEAEDDYL SFLISFGDFE DVILLSHTID SSSFENSLYH FAGKYYLYVT FNPDAPDREQ
DDLLAQLLEY GNDSDLSVYR IQEYGKTIVA EAALEHVQKY FKL
//
