ID I8AGR9_9BACI Unreviewed; 224 AA.
AC I8AGR9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Adapter protein MecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN Name=mecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN ORFNames=A374_14765 {ECO:0000313|EMBL:EIT84599.1};
OS Fictibacillus macauensis ZFHKF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT84599.1, ECO:0000313|Proteomes:UP000004080};
RN [1] {ECO:0000313|EMBL:EIT84599.1, ECO:0000313|Proteomes:UP000004080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT84599.1,
RC ECO:0000313|Proteomes:UP000004080};
RX PubMed=22887677; DOI=10.1128/JB.01049-12;
RA Cai L., Zhang T.;
RT "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL J. Bacteriol. 194:4780-4780(2012).
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:EIT84599.1}.
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DR EMBL; AKKV01000031; EIT84599.1; -; Genomic_DNA.
DR RefSeq; WP_007203029.1; NZ_AKKV01000031.1.
DR AlphaFoldDB; I8AGR9; -.
DR STRING; 1196324.A374_14765; -.
DR PATRIC; fig|1196324.3.peg.3017; -.
DR eggNOG; COG4862; Bacteria.
DR OrthoDB; 2360201at2; -.
DR Proteomes; UP000004080; 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:UP000004080};
KW Sporulation {ECO:0000256|HAMAP-Rule:MF_01124}.
SQ SEQUENCE 224 AA; 26430 MW; C31DAFC1AF8BE431 CRC64;
MEIERVNEFT IKFFITYGDI EDRGFDREEI WSNRERGEEL FWEMMDEAHQ QEQFPLEGPL
WIQVQALDKG LEIIVTRAQM SKDGTKLELP LGEEKIDLPV DKSIESLLDQ PFSSEEDSDH
EEIELADEDY LSFLLVFNDF EDLIMLSHNV DSSLFANSLY HFEHKYYLYV TFHQETTDRE
QDDLLSQLLE YGIDSDSSVH RIQEYGKQII ADRALEDISS HFPM
//
